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Information on SUBCLASS 4.1.1
Subclass Accession number: 36
Subclass: 4.1.1
Type: EH beta-alpha
DB: ArchDB-KI
Number of loops: 21

Average sequence ID (%) : 24.6 +/- 4.5
Average RMSD (Å) : 0.64 +/- 0.54

Consensus geometry
d (Å): 9 delta (°): 45-90 theta (°): 135-180 rho (°): 0-45
Consensus Sequence: hphppXhX
(φψ)-conformation: bpaabpaa
Pattern: xx{ILV}{DNQRST}{ACGY}[DENST]x[DPST][ILMPV]xx[CILV]{FIMVWY}x{DEKQS}[AILV]x{DEKNQT}
Conservation:-1.487-1.4551.4300.082-0.5380.684-0.4510.3810.0360.620-0.7841.926-0.257-0.5600.1011.625-1.332-0.023
Loops included in this Subclass
LoopPDBChainStartEndSequenceSec StructRamachandran
1ak2_*_2081ak2   -209226SAIDASQTPDVVFASILAEEEETTS-HHHHHHHHHHbbbxaaxxaaaaaaaaaa
1ake_A_1921ake   A194211AKVDGTKPVAEVRADLEKEEEETTS-HHHHHHHHHHbxbxaax-aaaaaaaaaa
1aky_*_1971aky   -198215AGVDASQPPATVWADILNEEEETTS-HHHHHHHHHHbbbxaaxxaaaaaaaaaa
1ank_A_1921ank   A194211AKVDGTKPVAEVRADLEKEEEETTS-HHHHHHHHHHbxbxaaxxaaaaaaaaaa
1dek_A_2191dek   A219236LVITNDGSLEELFSKIKNEEEE--S-HHHHHHHHHHxbbxxabxaaaaaaaaaa
1dvr_A_1971dvr   A198215AGVDASQPPATVWADILNEEEETTS-HHHHHHHHHHbxbxaax-aaaaaaaaaa
1kim_A_3231kim   A325342FILDYDQSPAGCRDALLQEEEE-SS-HHHHHHHHHHbbbxaabxaaaaaaaaaa
1qf9_A_1691qf9   A170187KIIPANRDVNEVYNDVENEEEE-SS-HHHHHHHHHHbxb-aabxaaaaaaaaaa
1qhi_A_3231qhi   A325342FILDYDQSPAGCRDALLQEEEE-SS-HHHHHHHHHHbxbxaabxaaaaaaaaaa
1shk_A_1491shk   A149166YVVDATQPPAAIVCELMQEEEETTS-HHHHHHHHHHbbbxaaxxaaaaaaaaaa
1uke_*_1691uke   -170187KIIPANRDVNEVYNDVENEEEE-SS-HHHHHHHHHHbbb-aabxaaaaaaaaaa
1uky_*_1801uky   -181198VRVRCDRSVEDVYKDVQDEEEESSS-HHHHHHHHHHbxbxaabxaaaaaaaaaa
1ukz_*_1801ukz   -181198VRVRCDRSVEDVYKDVQDEEEE-SS-HHHHHHHHHHbxbxaabxaaaaaaaaaa
1vtk_*_3231vtk   -325342FILDYDQSPAGCRDALLQEEEE-SS-HHHHHHHHHHbbbxaabpaaaaaaaaaa
1zak_A_1881zak   A189206VKVQGDATVDAVFAKIDEEEEE-SS-HHHHHHHHHHbxbxaxbpaaaaaaaaaa
1zip_*_1921zip   -193210RNINGEQDMEKVFADIREEEEE-SS-HHHHHHHHHHbxbxaabxaaaaaaaaaa
2cmk_A_2002cmk   A201218VLDSTTLSIEQVIEKALQEEE-TT--HHHHHHHHHHxbxaaabxaaaaaaaaaa
2eck_A_1922eck   A194211AKVDGTKPVAEVRADLEKEEEETTS-HHHHHHHHHHbbbxaapxaaaaaaaaaa
2ki5_A_3232ki5   A325342FILDYDQSPAGCRDALLQEEEE-SS-HHHHHHHHHHbbbxaabxaaaaaaaaaa
3adk_*_1703adk   -171188RKVNAEGSVDDVFSQVCTEEEE--S-HHHHHHHHHHbxbxabexaaaaaaaaaa
4tmk_*_1844tmk   -185202HTIDATQPLEAVMDAIRTEEEETTS-HHHHHHHHHHxxxxaax-aaaaaaaaaa
PDB ligands within a cut-off distance of 6 Å in this subclass
LoopPDBChainLigandsResidue
1ake_A_1921ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE G - 198
1ake_A_1921ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE T - 199
1ake_A_1921ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE K - 200
1ake_A_1921ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE P - 201
1ake_A_1921ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE V - 202
1ake_A_1921ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE A - 203
1ake_A_1921ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE V - 205
1aky_*_1971aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE A - 202
1aky_*_1971aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE S - 203
1aky_*_1971aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE Q - 204
1aky_*_1971aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE P - 205
1aky_*_1971aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE P - 206
1aky_*_1971aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE V - 209
1ank_A_1921ank   A     ANPPHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER D - 197
1ank_A_1921ank   A     ANPPHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER G - 198
1ank_A_1921ank   A     ANPPHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER T - 199
1ank_A_1921ank   A     ANPPHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER K - 200
1ank_A_1921ank   A     ANPPHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER P - 201
1ank_A_1921ank   A     ANPPHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER V - 202
1ank_A_1921ank   A     ANPPHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER E - 204
1ank_A_1921ank   A     ANPPHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER V - 205
1dvr_A_1971dvr   A     ATFPHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER A - 202
1dvr_A_1971dvr   A     ATFPHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER S - 203
1dvr_A_1971dvr   A     ATFPHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER Q - 204
1dvr_A_1971dvr   A     ATFPHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER P - 205
1dvr_A_1971dvr   A     ATFPHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER P - 206
1dvr_A_1971dvr   A     ATFPHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER V - 209
1qf9_A_1691qf9   A     ADPADENOSINE-5'-DIPHOSPHATE A - 174
1qf9_A_1691qf9   A     ADPADENOSINE-5'-DIPHOSPHATE N - 175
1qf9_A_1691qf9   A     ADPADENOSINE-5'-DIPHOSPHATE R - 176
1qf9_A_1691qf9   A     ADPADENOSINE-5'-DIPHOSPHATE D - 177
1qf9_A_1691qf9   A     ADPADENOSINE-5'-DIPHOSPHATE V - 178
1qf9_A_1691qf9   A     ADPADENOSINE-5'-DIPHOSPHATE N - 179
1qf9_A_1691qf9   A     ADPADENOSINE-5'-DIPHOSPHATE V - 181
1shk_A_1491shk   A     MGMAGNESIUM ION Y - 149
1shk_A_1491shk   A     MGMAGNESIUM ION V - 150
1uke_*_1691uke   *     UP5P1-(ADENOSINE-5'-P5-(URIDINE-5')PENTAPHOSPHATE A - 174
1uke_*_1691uke   *     UP5P1-(ADENOSINE-5'-P5-(URIDINE-5')PENTAPHOSPHATE N - 175
1uke_*_1691uke   *     UP5P1-(ADENOSINE-5'-P5-(URIDINE-5')PENTAPHOSPHATE R - 176
1uke_*_1691uke   *     UP5P1-(ADENOSINE-5'-P5-(URIDINE-5')PENTAPHOSPHATE D - 177
1uke_*_1691uke   *     UP5P1-(ADENOSINE-5'-P5-(URIDINE-5')PENTAPHOSPHATE V - 178
1uke_*_1691uke   *     UP5P1-(ADENOSINE-5'-P5-(URIDINE-5')PENTAPHOSPHATE N - 179
1uke_*_1691uke   *     UP5P1-(ADENOSINE-5'-P5-(URIDINE-5')PENTAPHOSPHATE E - 180
1uke_*_1691uke   *     UP5P1-(ADENOSINE-5'-P5-(URIDINE-5')PENTAPHOSPHATE V - 181
1uke_*_1691uke   *     UP5P1-(ADENOSINE-5'-P5-(URIDINE-5')PENTAPHOSPHATE Y - 182
1uky_*_1801uky   *     ADPADENOSINE-5'-DIPHOSPHATE C - 185
1uky_*_1801uky   *     ADPADENOSINE-5'-DIPHOSPHATE D - 186
1uky_*_1801uky   *     ADPADENOSINE-5'-DIPHOSPHATE R - 187
1uky_*_1801uky   *     ADPADENOSINE-5'-DIPHOSPHATE S - 188
1uky_*_1801uky   *     ADPADENOSINE-5'-DIPHOSPHATE V - 189
1uky_*_1801uky   *     ADPADENOSINE-5'-DIPHOSPHATE E - 190
1uky_*_1801uky   *     ADPADENOSINE-5'-DIPHOSPHATE V - 192
1ukz_*_1801ukz   *     ADPADENOSINE-5'-DIPHOSPHATE C - 185
1ukz_*_1801ukz   *     ADPADENOSINE-5'-DIPHOSPHATE D - 186
1ukz_*_1801ukz   *     ADPADENOSINE-5'-DIPHOSPHATE R - 187
1ukz_*_1801ukz   *     ADPADENOSINE-5'-DIPHOSPHATE S - 188
1ukz_*_1801ukz   *     ADPADENOSINE-5'-DIPHOSPHATE V - 189
1ukz_*_1801ukz   *     ADPADENOSINE-5'-DIPHOSPHATE E - 190
1ukz_*_1801ukz   *     ADPADENOSINE-5'-DIPHOSPHATE V - 192
1vtk_*_3231vtk   *     ADPADENOSINE-5'-DIPHOSPHATE Y - 329
1vtk_*_3231vtk   *     ADPADENOSINE-5'-DIPHOSPHATE Q - 331
1vtk_*_3231vtk   *     ADPADENOSINE-5'-DIPHOSPHATE S - 332
1vtk_*_3231vtk   *     ADPADENOSINE-5'-DIPHOSPHATE P - 333
1vtk_*_3231vtk   *     ADPADENOSINE-5'-DIPHOSPHATE A - 334
1vtk_*_3231vtk   *     ADPADENOSINE-5'-DIPHOSPHATE C - 336
1zak_A_1881zak   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE G - 193
1zak_A_1881zak   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE D - 194
1zak_A_1881zak   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE A - 195
1zak_A_1881zak   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE T - 196
1zak_A_1881zak   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE V - 197
1zak_A_1881zak   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE V - 200
1zip_*_1921zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE G - 197
1zip_*_1921zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE E - 198
1zip_*_1921zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE Q - 199
1zip_*_1921zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE D - 200
1zip_*_1921zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE M - 201
1zip_*_1921zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE V - 204
2eck_A_1922eck   A     ADPADENOSINE-5'-DIPHOSPHATE D - 197
2eck_A_1922eck   A     ADPADENOSINE-5'-DIPHOSPHATE G - 198
2eck_A_1922eck   A     ADPADENOSINE-5'-DIPHOSPHATE T - 199
2eck_A_1922eck   A     ADPADENOSINE-5'-DIPHOSPHATE K - 200
2eck_A_1922eck   A     ADPADENOSINE-5'-DIPHOSPHATE P - 201
2eck_A_1922eck   A     ADPADENOSINE-5'-DIPHOSPHATE V - 202
2eck_A_1922eck   A     ADPADENOSINE-5'-DIPHOSPHATE A - 203
2eck_A_1922eck   A     ADPADENOSINE-5'-DIPHOSPHATE E - 204
2eck_A_1922eck   A     ADPADENOSINE-5'-DIPHOSPHATE V - 205
Bibliographic annotations
LoopPDBChainAnnotationResidue
1ake_A_1921ake   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 RESIDUEK - 200
1ank_A_1921ank   RefM.B.BERRY,B.MEADOR,T.BILDERBACK,P.LIANG,M.GLASER,G.N.PHILLIPS JUNIOR. THE CLOSED CONFORMATION OF A HIGHLY FLEXIBLE PROTEIN: THE STRUCTURE OF E. COLI ADENYLATE KINASE WITH BOUND AMP AND AMPPNP  PROTEINS v.19;183,1994AATP BINDING RESIDUEK - 200
1ank_A_1921ank   RefM.B.BERRY,B.MEADOR,T.BILDERBACK,P.LIANG,M.GLASER,G.N.PHILLIPS JUNIOR. THE CLOSED CONFORMATION OF A HIGHLY FLEXIBLE PROTEIN: THE STRUCTURE OF E. COLI ADENYLATE KINASE WITH BOUND AMP AND AMPPNP  PROTEINS v.19;183,1994AATP BINDING RESIDUEP - 201
1ank_A_1921ank   RefM.B.BERRY,B.MEADOR,T.BILDERBACK,P.LIANG,M.GLASER,G.N.PHILLIPS JUNIOR. THE CLOSED CONFORMATION OF A HIGHLY FLEXIBLE PROTEIN: THE STRUCTURE OF E. COLI ADENYLATE KINASE WITH BOUND AMP AND AMPPNP  PROTEINS v.19;183,1994AATP BINDING RESIDUEV - 202
1dek_A_2191dek   RefA.TEPLYAKOV,P.SEBASTIAO,G.OBMOLOVA,A.PERRAKIS,G.S.BRUSH,M.J.BESSMAN,K.S.WILSON. CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 DEOXYNUCLEOTIDE KINASE WITH ITS SUBSTRATES DGMP AND ATP  EMBO J. v.15;3487,1996AATP BINDING RESIDUEL - 227
1dek_A_2191dek   RefA.TEPLYAKOV,P.SEBASTIAO,G.OBMOLOVA,A.PERRAKIS,G.S.BRUSH,M.J.BESSMAN,K.S.WILSON. CRYSTAL STRUCTURE OF BACTERIOPHAGE T4 DEOXYNUCLEOTIDE KINASE WITH ITS SUBSTRATES DGMP AND ATP  EMBO J. v.15;3487,1996AATP BINDING RESIDUEL - 230
1shk_A_1491shk   RefT.KRELL,J.E.COYLE,M.J.HORSBURGH,J.R.COGGINS,A.J.LAPTHORN. CRYSTALLIZATION AND PRELIMINARY X-RAY CRYSTALLOGRAPHIC ANALYSIS OF SHIKIMATE KINASE FROM ERWINIA CHRYSANTHEMI  ACTA CRYSTALLOGR.,SECT.D v.53;612,1997AATP BINDING RESIDUEA - 153
1shk_A_1491shk   RefT.KRELL,J.E.COYLE,M.J.HORSBURGH,J.R.COGGINS,A.J.LAPTHORN. CRYSTALLIZATION AND PRELIMINARY X-RAY CRYSTALLOGRAPHIC ANALYSIS OF SHIKIMATE KINASE FROM ERWINIA CHRYSANTHEMI  ACTA CRYSTALLOGR.,SECT.D v.53;612,1997AATP BINDING RESIDUEA - 153
1shk_A_1491shk   RefT.KRELL,J.E.COYLE,M.J.HORSBURGH,J.R.COGGINS,A.J.LAPTHORN. CRYSTALLIZATION AND PRELIMINARY X-RAY CRYSTALLOGRAPHIC ANALYSIS OF SHIKIMATE KINASE FROM ERWINIA CHRYSANTHEMI  ACTA CRYSTALLOGR.,SECT.D v.53;612,1997AATP BINDING RESIDUEA - 158
2eck_A_1922eck   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;276,1998AATP BINDING RESIDUEK - 200
2eck_A_1922eck   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;276,1998AATP BINDING RESIDUEP - 201
2eck_A_1922eck   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;276,1998AATP BINDING RESIDUEV - 202

Clusters included in this Subclass
CLUSTER: EH.3.9
CLUSTER: EH.4.11