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Information on SUBCLASS 4.1.1
Subclass Accession number: 74
Subclass: 4.1.1
Type: HA beta-beta hairpin
DB: ArchDB-KI
Number of loops: 58

Average sequence ID (%) : 14.1 +/- 2.7
Average RMSD (Å) : 1.12 +/- 0.60

Consensus geometry
d (Å): 3 delta (°): 90-135 theta (°): 90-135 rho (°): 270-315
Consensus Sequence: hXXXphXX
(φψ)-conformation: bbpaagbb
Pattern: {ACGILMVW}xxxx{DENQSTY}x{DEHKNQRSTY}xx
Conservation:0.7790.032-0.665-0.2210.0012.447-0.519-0.092-1.084-0.677
Loops included in this Subclass
LoopPDBChainStartEndSequenceSec StructRamachandran
1a06_*_341a06   -3746AEDKRTQKLVEEETTT--EEbbxaaavxxb
1a6o_*_1621a6o   -163172MIDHELRKLREEETTTTEEExbbaaalbbb
1a6o_*_971a6o   -101110VRDQHSKTPSEE-TTT--EEbbxaaavxxb
1ad5_A_1181ad5   A121130ARSLATRKEGEEETTT--EEbbxaaavxbe
1ad5_A_3921ad5   A392401ILVSASLVCKEEE-TT--EEbbbxaavxxb
1ak2_*_1441ak2   -144153LIHPQSGRSYEE-TTT--EEbbxaaavpbb
1ake_A_1231ake   A124133RVHAPSGRVYEEETTTTEEEbbxaaavxbb
1aky_*_1321aky   -133142LIHPASGRSYEE-TTT--EEbbxaaNgpbb
1apm_E_1721apm   E172181LLIDQQGYIQEEE-TTS-EEbbxxaavxxb
1apm_E_551apm   E6069VKHKESGNHYEEETTT--EEbbxaaavxxb
1aq1_*_1331aq1   -133142LLINTEGAIKEEE-TTS-EEbbbbaagxbb
1b38_A_1331b38   A133142LLINTEGAIKEEE-TTS-EEbbbbaavxbb
1b6c_B_3391b6c   B339348ILVKKNGTCCEEE-TTS-EEbbbxaavbbb
1b6c_B_3561b6c   B356365VRHDSATDTIEEEETTTTEEbbbbaaNlbb
1blx_A_1511blx   A151160ILVTSSGQIKEEE-TT--EEbxbxaavxxb
1bu6_O_151bu6   O1928VVMDHDANIIEEE-TTS-EEbbbxaavbxa
1bu6_O_1921bu6   O192199.FNIHTLDW..EETTTTEE..bxaaalbp.
1bu6_O_861bu6   O8897VWEKETGKPIEEETTTTEEEbbbaaavxxa
1bx4_A_2691bx4   A272281IMATESEVTAEEE-SS-EEEbbbbaabbbb
1byg_A_3201byg   A320329VLVSEDNVAKEEE-TTS-EEbbbxaavbxb
1c3q_A_1721c3q   A173182VIADTSHVYTEEE-SS-EEEbbbbaabbbb
1cdk_A_1721cdk   A172181LLIDQQGYIQEEE-TTS-EEbbbxaavxxb
1cdk_A_561cdk   A6069VKHKETGNHFEEETTT--EEbbxaaavxxb
1ckp_*_1331ckp   -133142LLINTEGAIKEEE-TTS-EEMbbbaavxbb
1ckp_*_161ckp   -2130ARNKLTGEVVEEETTT--EEbbxaaavxxb
1dvr_A_1321dvr   A133142LIHPASGRSYEEETTTTEEEbbxaaavxbb
1erk_*_1531erk   -153162LLLNTTCDLKEEE-TT--EEbxbbaavxxb
1fgk_A_6291fgk   A629638VLVTEDNVMKEEE-TT--EEbbbxaavxxb
1hcl_*_1331hcl   -133142LLINTEGAIKEEE-TTS-EEbbbbaavxbb
1hcl_*_171hcl   -2130ARNKLTGEVVEEETTT--EEbbxaaavxxb
1ir3_A_11381ir3   A11381147CMVAHDFTVKEEE-TT--EEbbbxaavxxb
1irk_*_11381irk   -11381147CMVAHDFTVKEEE-TT--EEbbbxaavxbb
1jnk_*_1951jnk   -195204IVVKSDCTLKEEE-TTS-EEbbbbaavxbb
1jsu_A_1331jsu   A133142LLINTEGAIKEEE-TTS-EEbxbbaagxbb
1koa_*_59541koa   -59595968VTERATGNNFEEETTTTEEEbbxaaavbxb
1koa_*_63361koa   -63396348RAKNSYGTKEEEEETTEEEEbbbbaabbbb
1kob_A_651kob   A7079CVEKATGRVFEEETTT--EEbbxaaavxxb
1p38_*_1561p38   -156165LAVNEDCELKEEE-TT--EEbxbxaavxbb
1p38_*_361p38   -4150AFDTKTGHRVEEETTT--EEbxxaaavxxb
1phk_*_1551phk   -155164ILLDDDMNIKEEE-TT--EEbbbxaavxxb
1pme_*_391pme   -4251AYDNVNKVRVEEETTT-SEEbbxaaalbxb
1rkd_*_961rkd   -100109IFVNGEGENVEEE-TTS-EEbbbxaavxbb
1tki_A_361tki   A4150CVETSSKKTYEEETTTTEEEbbxaaavxxb
1tki_A_831tki   A8695SFESMEELVMEEEETTEEEEbbbbaabbbb
1wfc_*_1561wfc   -156165LAVNEDCELKEEE-TTS-EEbbbxaavxbb
1ydr_E_1721ydr   E172181LLIDQQGYIQEEE-TTS-EEbbxxaavxxb
1zak_A_1291zak   A130139RLDPVTGKIYEE-TTT--EEbbxaaagxxb
1zip_*_1271zip   -128137RICRNCGATYEEETTT--EEbbxaaavpbb
2ak3_A_1262ak3   A127136WIHPGSGRVYEEETTTTEEEbbxaaavxbb
2csn_*_242csn   -2938GTNLLNNQQVEEETTT--EEbbxaaavxxb
2eck_A_1232eck   A124133RVHAPSGRVYEEETTTTEEEbbbaaavxbb
2fgi_A_6292fgi   A629638VLVTEDNVMKEEE-TT--EEbbbxaavxxb
2ptk_*_1182ptk   -121130AHSLTTGQTGEEETTT--EEbbxaaavxbe
2ptk_*_1992ptk   -204213IRKLDSGGFYEEE-TTS-EEbxxpaagpbb
2ptk_*_3922ptk   -392401ILVGENLVCKEEE-TTS-EEbbbbaxlxbb
2src_*_1182src   -121130AHSLSTGQTGEEETTT--EEbbxaaavxbe
2src_*_1962src   -204213IRKLDSGGFYEEE-SSS-EEbbbpaaNpbb
3lck_*_3703lck   -370379ILVSDTLSCKEEE-TTS-EEbbbxaavbbb
PDB ligands within a cut-off distance of 6 Å in this subclass
LoopPDBChainLigandsResidue
1ad5_A_3921ad5   A     ANPPHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER L - 393
1ake_A_1231ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 123
1ake_A_1231ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 124
1ake_A_1231ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE V - 132
1ake_A_1231ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE Y - 133
1ake_A_1231ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE H - 134
1aky_*_1321aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 132
1aky_*_1321aky   *     IMDIMIDAZOLE R - 132
1aky_*_1321aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE L - 133
1aky_*_1321aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE I - 134
1aky_*_1321aky   *     IMDIMIDAZOLE G - 139
1aky_*_1321aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE S - 141
1aky_*_1321aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE Y - 142
1aky_*_1321aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE H - 143
1aq1_*_1331aq1   *     STUSTAUROSPORINE L - 133
1aq1_*_1331aq1   *     STUSTAUROSPORINE L - 134
1b38_A_1331b38   A     ATPADENOSINE-5'-TRIPHOSPHATE L - 133
1b38_A_1331b38   A     ATPADENOSINE-5'-TRIPHOSPHATE L - 134
1bx4_A_2691bx4   A     ADNADENOSINE D - 269
1bx4_A_2691bx4   A     ADNADENOSINE T - 271
1dvr_A_1321dvr   A     ATFPHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER R - 132
1dvr_A_1321dvr   A     ATFPHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER L - 133
1dvr_A_1321dvr   A     ATFPHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER I - 134
1dvr_A_1321dvr   A     ATFPHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER S - 141
1dvr_A_1321dvr   A     ATFPHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER Y - 142
1dvr_A_1321dvr   A     ATFPHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER H - 143
1phk_*_1551phk   *     ATPADENOSINE-5'-TRIPHOSPHATE L - 156
1rkd_*_961rkd   *     RIBRIBOSE V - 97
1rkd_*_961rkd   *     PO4PHOSPHATE ION V - 97
1rkd_*_961rkd   *     RIBRIBOSE A - 98
1rkd_*_961rkd   *     RIBRIBOSE I - 100
1rkd_*_961rkd   *     RIBRIBOSE I - 110
1rkd_*_961rkd   *     RIBRIBOSE I - 112
1ydr_E_1721ydr   E     IQP1-(5-ISOQUINOLINESULFONYL)-2-METHYLPIPERAZINE L - 172
1ydr_E_1721ydr   E     IQP1-(5-ISOQUINOLINESULFONYL)-2-METHYLPIPERAZINE L - 173
1zak_A_1291zak   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 129
1zak_A_1291zak   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 130
1zak_A_1291zak   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE I - 138
1zak_A_1291zak   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE Y - 139
1zak_A_1291zak   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE H - 140
1zip_*_1271zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 127
1zip_*_1271zip   *     MNMANGANESE (II) ION R - 127
1zip_*_1271zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 128
1zip_*_1271zip   *     ZNZINC ION C - 130
1zip_*_1271zip   *     ZNZINC ION R - 131
1zip_*_1271zip   *     ZNZINC ION N - 132
1zip_*_1271zip   *     ZNZINC ION C - 133
1zip_*_1271zip   *     ZNZINC ION G - 134
1zip_*_1271zip   *     ZNZINC ION A - 135
1zip_*_1271zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE T - 136
1zip_*_1271zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE Y - 137
1zip_*_1271zip   *     ZNZINC ION Y - 137
1zip_*_1271zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE H - 138
2csn_*_242csn   *     CKIN-(2-AMINOETHYL)-5-CHLOROISOQUINOLINE-8-SULFONAMIDE I - 26
2csn_*_242csn   *     CKIN-(2-AMINOETHYL)-5-CHLOROISOQUINOLINE-8-SULFONAMIDE A - 39
2csn_*_242csn   *     CKIN-(2-AMINOETHYL)-5-CHLOROISOQUINOLINE-8-SULFONAMIDE K - 41
2eck_A_1232eck   A     AMPADENOSINE MONOPHOSPHATE R - 123
2eck_A_1232eck   A     ADPADENOSINE-5'-DIPHOSPHATE R - 123
2eck_A_1232eck   A     ADPADENOSINE-5'-DIPHOSPHATE R - 124
2eck_A_1232eck   A     ADPADENOSINE-5'-DIPHOSPHATE V - 132
2eck_A_1232eck   A     ADPADENOSINE-5'-DIPHOSPHATE Y - 133
2eck_A_1232eck   A     ADPADENOSINE-5'-DIPHOSPHATE H - 134
2ptk_*_1992ptk   *     PTRO-PHOSPHOTYROSINE H - 201
2ptk_*_1992ptk   *     PTRO-PHOSPHOTYROSINE Y - 202
2ptk_*_1992ptk   *     PTRO-PHOSPHOTYROSINE K - 203
PDB Site Annotated loops in this subclass
LoopPDBChainSiteResidue
1rkd_*_961rkd   * RB3RESIDUES WITHIN VAN DER WAALS DISTANCE OF RIBOSE.A - 98
1rkd_*_961rkd   * RB3RESIDUES WITHIN VAN DER WAALS DISTANCE OF RIBOSE.I - 100
1rkd_*_961rkd   * RB3RESIDUES WITHIN VAN DER WAALS DISTANCE OF RIBOSE.I - 110
1rkd_*_961rkd   * RB3RESIDUES WITHIN VAN DER WAALS DISTANCE OF RIBOSE.I - 112
1zip_*_1271zip   * ZFZINC FINGER RESIDUES.C - 130
1zip_*_1271zip   * ZFZINC FINGER RESIDUES.C - 133
Bibliographic annotations
LoopPDBChainAnnotationResidue
1ake_A_1231ake   RefC.W.MUELLER,G.E.SCHULZ. STRUCTURE OF THE COMPLEX BETWEEN ADENYLATE KINASE FROM ESCHERICHIA COLI AND THE INHIBITOR AP=5=A REFINED AT 1.9 ANGSTROMS RESOLUTION: A MODEL FOR A CATALYTIC TRANSITION STATE  J.MOL.BIOL. v.224;159,1992AP-ATP BINDING RESIDUER - 123
1ake_A_1231ake   RefC.W.MUELLER,G.E.SCHULZ. STRUCTURE OF THE COMPLEX BETWEEN ADENYLATE KINASE FROM ESCHERICHIA COLI AND THE INHIBITOR AP=5=A REFINED AT 1.9 ANGSTROMS RESOLUTION: A MODEL FOR A CATALYTIC TRANSITION STATE  J.MOL.BIOL. v.224;159,1992AATP BINDING RESIDUEY - 133
1apm_E_551apm   RefD.R.KNIGHTON,S.M.BELL,J.ZHENG,L.F.TEN *EYCK,N.-H.XUONG,S.S.TAYLOR,J.M.SOWADSKI. 2.0 ANGSTROM REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH A PEPTIDE INHIBITOR AND DETERGENT  ACTA CRYSTALLOGR D BIOL CRYSTALLOG v.49;357,1993EGLY-RICH-LOOPG - 55
1apm_E_551apm   RefD.R.KNIGHTON,S.M.BELL,J.ZHENG,L.F.TEN *EYCK,N.-H.XUONG,S.S.TAYLOR,J.M.SOWADSKI. 2.0 ANGSTROM REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH A PEPTIDE INHIBITOR AND DETERGENT  ACTA CRYSTALLOGR D BIOL CRYSTALLOG v.49;357,1993EP-ATP BINDING RESIDUEG - 55
1apm_E_551apm   RefD.R.KNIGHTON,S.M.BELL,J.ZHENG,L.F.TEN *EYCK,N.-H.XUONG,S.S.TAYLOR,J.M.SOWADSKI. 2.0 ANGSTROM REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH A PEPTIDE INHIBITOR AND DETERGENT  ACTA CRYSTALLOGR D BIOL CRYSTALLOG v.49;357,1993EADENINE BINDING RESIDUEV - 57
1apm_E_551apm   RefD.R.KNIGHTON,S.M.BELL,J.ZHENG,L.F.TEN *EYCK,N.-H.XUONG,S.S.TAYLOR,J.M.SOWADSKI. 2.0 ANGSTROM REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH A PEPTIDE INHIBITOR AND DETERGENT  ACTA CRYSTALLOGR D BIOL CRYSTALLOG v.49;357,1993EADENINE BINDING RESIDUEA - 70
1apm_E_551apm   RefD.R.KNIGHTON,S.M.BELL,J.ZHENG,L.F.TEN *EYCK,N.-H.XUONG,S.S.TAYLOR,J.M.SOWADSKI. 2.0 ANGSTROM REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH A PEPTIDE INHIBITOR AND DETERGENT  ACTA CRYSTALLOGR D BIOL CRYSTALLOG v.49;357,1993EADENINE BINDING RESIDUEA - 70
1apm_E_1721apm   RefD.R.KNIGHTON,S.M.BELL,J.ZHENG,L.F.TEN *EYCK,N.-H.XUONG,S.S.TAYLOR,J.M.SOWADSKI. 2.0 ANGSTROM REFINED CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE COMPLEXED WITH A PEPTIDE INHIBITOR AND DETERGENT  ACTA CRYSTALLOGR D BIOL CRYSTALLOG v.49;357,1993EADENINE BINDING RESIDUEL - 173
1b6c_B_3561b6c   RefM.HUSE,Y.G.CHEN,J.MASSAGUE,J.KURIYAN. CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF THE TYPE I TGF BETA RECEPTOR IN COMPLEX WITH FKBP12  CELL(CAMBRIDGE,MASS.) v.96;425,1999BPHOSPHORYLATION SITER - 357
1b6c_B_3561b6c   RefM.HUSE,Y.G.CHEN,J.MASSAGUE,J.KURIYAN. CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF THE TYPE I TGF BETA RECEPTOR IN COMPLEX WITH FKBP12  CELL(CAMBRIDGE,MASS.) v.96;425,1999BPHOSPHORYLATION SITE(HIPOTETIC)T - 362
1b6c_B_3561b6c   RefM.HUSE,Y.G.CHEN,J.MASSAGUE,J.KURIYAN. CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF THE TYPE I TGF BETA RECEPTOR IN COMPLEX WITH FKBP12  CELL(CAMBRIDGE,MASS.) v.96;425,1999BPHOSPHORYLATION SITE(HIPOTETIC)T - 364
1c3q_A_1721c3q   RefN.CAMPOBASSO,I.I.MATHEWS,T.P.BEGLEY,S.E.EALICK. CRYSTAL STRUCTURE OF 4-METHYL-5-BETA-HYDROXYETHYLTHIAZOLE KINASE FROM BACILLUS SUBTILIS AT 1.5 A RESOLUTION  BIOCHEMISTRY v.39;7868,2000ARIBOSE BINDING RESIDUED - 172
1cdk_A_561cdk   RefD.BOSSEMEYER,R.A.ENGH,V.KINZEL,H.PONSTINGL,R.HUBER. PHOSPHOTRANSFERASE AND SUBSTRATE BINDING MECHANISM OF THE CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT FROM PORCINE HEART AS DEDUCED FROM THE 2.0 ANGSTROMS STRUCTURE OF THE COMPLEX WITH MN==2+== ADENYLYL IMIDODIPHOSPHATE AND INHIBITOR PEPTIDE PKI(5-24)  EMBO J. v.12;849,1993AADENINE BINDING RESIDUEV - 57
1cdk_A_561cdk   RefD.BOSSEMEYER,R.A.ENGH,V.KINZEL,H.PONSTINGL,R.HUBER. PHOSPHOTRANSFERASE AND SUBSTRATE BINDING MECHANISM OF THE CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT FROM PORCINE HEART AS DEDUCED FROM THE 2.0 ANGSTROMS STRUCTURE OF THE COMPLEX WITH MN==2+== ADENYLYL IMIDODIPHOSPHATE AND INHIBITOR PEPTIDE PKI(5-24)  EMBO J. v.12;849,1993AGLY-RICH-LOOPV - 57
1cdk_A_1721cdk   RefD.BOSSEMEYER,R.A.ENGH,V.KINZEL,H.PONSTINGL,R.HUBER. PHOSPHOTRANSFERASE AND SUBSTRATE BINDING MECHANISM OF THE CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT FROM PORCINE HEART AS DEDUCED FROM THE 2.0 ANGSTROMS STRUCTURE OF THE COMPLEX WITH MN==2+== ADENYLYL IMIDODIPHOSPHATE AND INHIBITOR PEPTIDE PKI(5-24)  EMBO J. v.12;849,1993AATP BINDING RESIDUEL - 172
1cdk_A_1721cdk   RefD.BOSSEMEYER,R.A.ENGH,V.KINZEL,H.PONSTINGL,R.HUBER. PHOSPHOTRANSFERASE AND SUBSTRATE BINDING MECHANISM OF THE CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT FROM PORCINE HEART AS DEDUCED FROM THE 2.0 ANGSTROMS STRUCTURE OF THE COMPLEX WITH MN==2+== ADENYLYL IMIDODIPHOSPHATE AND INHIBITOR PEPTIDE PKI(5-24)  EMBO J. v.12;849,1993AADENINE BINDING RESIDUEL - 173
1fgk_A_6291fgk   RefM.MOHAMMADI, J.SCHLESSINGER, S.R.HUBBARD. STRUCTURE OF THE FGF RECEPTOR TYROSINE KINASE DOMAIN REVEALS A NOVEL AUTOINHIBITORY MECHANISM  CELL v.86;577,1996AATP BINDING RESIDUEL - 630
1ir3_A_11381ir3   RefS.R.HUBBARD. CRYSTAL STRUCTURE OF THE ACTIVATED INSULIN RECEPTOR TYROSINE KINASE IN COMPLEX WITH PEPTIDE SUBSTRATE AND ATP ANALOG  EMBO J. v.16;5572,1997ACATALYTIC LOOPC - 1138
1ir3_A_11381ir3   RefS.R.HUBBARD. CRYSTAL STRUCTURE OF THE ACTIVATED INSULIN RECEPTOR TYROSINE KINASE IN COMPLEX WITH PEPTIDE SUBSTRATE AND ATP ANALOG  EMBO J. v.16;5572,1997ACATALYTIC LOOPC - 1138
1ir3_A_11381ir3   RefS.R.HUBBARD. CRYSTAL STRUCTURE OF THE ACTIVATED INSULIN RECEPTOR TYROSINE KINASE IN COMPLEX WITH PEPTIDE SUBSTRATE AND ATP ANALOG  EMBO J. v.16;5572,1997AADENINE BINDING RESIDUEM - 1139
1jsu_A_1331jsu   RefA.A.RUSSO,P.D.JEFFREY,A.K.PATTEN,J.MASSAGUE,N.P.PAVLETICH. CRYSTAL STRUCTURE OF THE P27KIP1 CYCLIN-DEPENDENT-KINASE INHIBITOR BOUND TO THE CYCLIN A-CDK2 COMPLEX  NATURE v.382;325,1996AP27 PROTEIN BINDING RESIDUEL - 134
1kob_A_651kob   RefB.KOBE,J.HEIERHORST,S.C.FEIL,M.W.PARKER,G.M.BENIAN,K.R.WEISS,B.E.KEMP. GIANT PROTEIN KINASES: DOMAIN INTERACTIONS AND STRUCTURAL BASIS OF AUTOREGULATION  EMBO J. v.15;6810,1996AGLY-RICH-LOOPG - 65
1kob_A_651kob   RefB.KOBE,J.HEIERHORST,S.C.FEIL,M.W.PARKER,G.M.BENIAN,K.R.WEISS,B.E.KEMP. GIANT PROTEIN KINASES: DOMAIN INTERACTIONS AND STRUCTURAL BASIS OF AUTOREGULATION  EMBO J. v.15;6810,1996AP-ATP BINDING RESIDUEK - 82
1zak_A_1291zak   RefK.WILD,R.GRAFMULLER,E.WAGNER,G.E.SCHULZ. STRUCTURE, CATALYSIS AND SUPRAMOLECULAR ASSEMBLY OF ADENYLATE KINASE FROM MAIZE  EUR.J.BIOCHEM. v.250;326,1997AP-ATP BINDING RESIDUER - 129
2eck_A_1232eck   RefM.B.BERRY,T.BILDERBACK,M.GLASER,G.N.PHILLIPS JUNIOR. A CRYSTAL STRUCTURE OF E. COLI ADENYLATE KINASE WITH BOUND AMP AND ADP  PROTEINS v.15;276,1998AP-ATP BINDING RESIDUER - 123
2fgi_A_6292fgi   RefM.MOHAMMADI,S.FROUM,J.M.HAMBY,M.C.SCHROEDER,R.L.PANEK,G.H.LU,A.V.ELISEENKOVA,D.GREEN,J.SCHLESSINGER,S.R.HUBBARD. CRYSTAL STRUCTURE OF AN ANGIOGENESIS INHIBITOR BOUND TO THE FGF RECEPTOR TYROSINE KINASE DOMAIN  EMBO J. v.17;5896,1998AADENINE BINDING RESIDUEL - 630

Clusters included in this Subclass
CLUSTER: HA.3.2
CLUSTER: HA.4.0
CLUSTER: HA.4.1
CLUSTER: HA.4.13
CLUSTER: HA.4.14
CLUSTER: HA.4.15
CLUSTER: HA.4.3
CLUSTER: HA.5.0
CLUSTER: HA.5.1
CLUSTER: HA.5.5
CLUSTER: HA.6.0
CLUSTER: HA.6.1
CLUSTER: HA.7.0