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Information on SUBCLASS 0.1.1
Subclass Accession number: 88
Subclass: 0.1.1
Type: HE alpha-beta
DB: ArchDB-KI
 Number of loops: 7

Average sequence ID (%) : 61.0 +/- 4.0
Average RMSD (Å) : 0.16 +/- 0.03

Consensus geometry
d (Å): 5 delta (°): 0-45 theta (°): 45-90 rho (°): 90-135
Consensus Sequence: XGRX
(φψ)-conformation: aabb
Pattern: [IL][MV]{AE}[R][ILV][TV][G][R]{R}[ILV]
Conservation:-0.145-0.355-1.1091.131-0.338-0.6891.7931.131-1.065-0.353
Loops included in this Subclass
LoopPDBChainStartEndSequenceSec StructRamachandran
1ake_A_1161ake   A116125IVDRIVGRRVHHHHHHTEEEaaaaaaaxbb
1aky_*_1221aky   -125134LVARITGRLIHHHHHHTEEEaaaaaaaxbb
1ank_A_1161ank   A116125IVDRIVGRRVHHHHHHTEEEaaaaaaaxbb
1dvr_A_1221dvr   A125134LVARITGRLIHHHHHHTEEEaaaaaaaxbb
1zak_A_1191zak   A122131LVERVVGRRLHHHHHTTEEEaaaaaaaxbb
1zip_*_1171zip   -120129LMERLTGRRIHHHHHHTEEEaaaaaaaxbb
2eck_A_1132eck   A116125IVDRIVGRRVHHHHHHTEEEaaaaaaabbb
PDB ligands within a cut-off distance of 6 Å in this subclass
LoopPDBChainLigandsResidue
1ake_A_1161ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 119
1ake_A_1161ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE I - 120
1ake_A_1161ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE G - 122
1ake_A_1161ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 123
1ake_A_1161ake   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 124
1aky_*_1221aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 128
1aky_*_1221aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE I - 129
1aky_*_1221aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE G - 131
1aky_*_1221aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 132
1aky_*_1221aky   *     IMDIMIDAZOLE R - 132
1aky_*_1221aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE L - 133
1aky_*_1221aky   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE I - 134
1ank_A_1161ank   A     ANPPHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER R - 119
1ank_A_1161ank   A     ANPPHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER I - 120
1ank_A_1161ank   A     ANPPHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER G - 122
1ank_A_1161ank   A     AMPADENOSINE MONOPHOSPHATE R - 123
1ank_A_1161ank   A     ANPPHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER R - 123
1ank_A_1161ank   A     ANPPHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER R - 124
1ank_A_1161ank   A     ANPPHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER V - 125
1dvr_A_1221dvr   A     ATFPHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER R - 128
1dvr_A_1221dvr   A     ATFPHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER I - 129
1dvr_A_1221dvr   A     ATFPHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER G - 131
1dvr_A_1221dvr   A     ATFPHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER R - 132
1dvr_A_1221dvr   A     ATFPHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER L - 133
1dvr_A_1221dvr   A     ATFPHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER I - 134
1zak_A_1191zak   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 125
1zak_A_1191zak   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE V - 126
1zak_A_1191zak   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE G - 128
1zak_A_1191zak   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 129
1zak_A_1191zak   A     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 130
1zip_*_1171zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 123
1zip_*_1171zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE L - 124
1zip_*_1171zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE G - 126
1zip_*_1171zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 127
1zip_*_1171zip   *     MNMANGANESE (II) ION R - 127
1zip_*_1171zip   *     AP5BIS(ADENOSINE)-5'-PENTAPHOSPHATE R - 128
1zip_*_1171zip   *     ZNZINC ION C - 130
2eck_A_1132eck   A     ADPADENOSINE-5'-DIPHOSPHATE R - 119
2eck_A_1132eck   A     ADPADENOSINE-5'-DIPHOSPHATE I - 120
2eck_A_1132eck   A     ADPADENOSINE-5'-DIPHOSPHATE G - 122
2eck_A_1132eck   A     AMPADENOSINE MONOPHOSPHATE R - 123
2eck_A_1132eck   A     ADPADENOSINE-5'-DIPHOSPHATE R - 123
2eck_A_1132eck   A     ADPADENOSINE-5'-DIPHOSPHATE R - 124
PDB Site Annotated loops in this subclass
LoopPDBChainSiteResidue
1zip_*_1171zip   * ZFZINC FINGER RESIDUES.C - 130
Bibliographic annotations
LoopPDBChainAnnotationResidue
1ake_A_1161ake   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 RESIDUER - 119
1ake_A_1161ake   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
1ank_A_1161ank   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;183,1994AP-ATP BINDING RESIDUER - 123
1zak_A_1191zak   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_1132eck   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

Clusters included in this Subclass
CLUSTER: HE.1.3