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Information on SUBCLASS 3.1.3
Subclass Accession number: 116
Subclass: 3.1.3
Type: HE alpha-beta
DB: ArchDB-KI
 Number of loops: 5

Average sequence ID (%) : 8.2 +/- 0.4
Average RMSD (Å) : 0.90 +/- 0.28

Consensus geometry
d (Å): 9 delta (°): 90-135 theta (°): 135-180 rho (°): 0-45
Consensus Sequence: phXhpXh
(φψ)-conformation: aalpabb
Pattern: x{ALMV}{AGV}x[DEKN][AFLM][ACIL]{DEHK}[DEK]{FMV}[GN]{AIL}{DEKN}x{FGV}{FMVY}{ACI}
Conservation:-1.146-0.1440.171-0.5081.0310.3450.206-0.5541.707-0.4202.606-0.4360.174-0.873-1.205-0.281-0.673
Loops included in this Subclass
LoopPDBChainStartEndSequenceSec StructRamachandran
1dku_A_2301dku   A233249TLAANALVENGAKEVYAHHHHHHHHHTT-SEEEEaaaaaaaaaagxabbbb
1e19_A_2151e19   A217233LAGEKLAEEVNADIFMIHHHHHHHHHTT-SEEEEaaaaaaaaaalxabbbx
1h72_C_631h72   C6682IVAKKMIDDFNIGKGVKHHHHHHHHHTT---EEEaaaaaaaaaalxabbbb
1i58_B_3651i58   B367383RMVRDLAKKMNKEVNFIHHHHHHHHHTT--EEEEaaaaaaaaaalbbbbxb
1kbl_A_8381kbl   A838854PSSVEFCHKVGLNYVSCHHHHHHHHHTT-SEEEEaaaaaaaaaavxabbbb
PDB ligands within a cut-off distance of 6 Å in this subclass
LoopPDBChainLigandsResidue
1e19_A_2151e19   A     ADPADENOSINE-5'-DIPHOSPHATE K - 215
1e19_A_2151e19   A     MGMAGNESIUM ION K - 215
1e19_A_2151e19   A     ADPADENOSINE-5'-DIPHOSPHATE D - 216
1e19_A_2151e19   A     MGMAGNESIUM ION D - 216
1e19_A_2151e19   A     ADPADENOSINE-5'-DIPHOSPHATE L - 234
1e19_A_2151e19   A     ADPADENOSINE-5'-DIPHOSPHATE T - 235
PDB Site Annotated loops in this subclass
LoopPDBChainSiteResidue
1h72_C_631h72   C TRSTRS BINDING SITE FOR CHAIN CD - 73
1h72_C_631h72   C TRSTRS BINDING SITE FOR CHAIN CN - 76
Bibliographic annotations
LoopPDBChainAnnotationResidue
1e19_A_2151e19   RefS.RAMON-MAIQUES,A.MARINA,M.URIARTE,I.FITA,V.RUBIO. THE 1.5-A RESOLUTION CRYSTAL STRUCTURE OF THE CARBAMATE KINASE-LIKE CARBAMOYL PHOSPHATE SYNTHETASE FROM THE HYPERTHERMOPHILIC ARCHAEON PYROCOCCUS FURIOSUS, BOUND TO ADP, CONFIRMS THAT THIS THERMOESTABLE ENZYME IS A CARBAMATE KINASE, AND PROVIDES INSIGHTS INTO SUBSTRATE BINDING AND STABILITY IN CARBAMATE KINASES  J.MOL.BIOL. v.299;463,2000ACATALYTIC RESIDUEK - 215
1e19_A_2151e19   RefS.RAMON-MAIQUES,A.MARINA,M.URIARTE,I.FITA,V.RUBIO. THE 1.5-A RESOLUTION CRYSTAL STRUCTURE OF THE CARBAMATE KINASE-LIKE CARBAMOYL PHOSPHATE SYNTHETASE FROM THE HYPERTHERMOPHILIC ARCHAEON PYROCOCCUS FURIOSUS, BOUND TO ADP, CONFIRMS THAT THIS THERMOESTABLE ENZYME IS A CARBAMATE KINASE, AND PROVIDES INSIGHTS INTO SUBSTRATE BINDING AND STABILITY IN CARBAMATE KINASES  J.MOL.BIOL. v.299;463,2000AREGULATORY ADP BINDING RESIDUET - 235
1h72_C_631h72   RefS.S.KRISHNA,T.ZHOU,M.DAUGHERTY,A.OSTERMAN,H.ZHANG. STRUCTURAL BASIS FOR THE CATALYSIS AND SUBSTRATE SPECIFICITY OF HOMOSERINE KINASE  BIOCHEMISTRY v.40;10810,2001CATP BINDING RESIDUEV - 63

Clusters included in this Subclass
CLUSTER: HE.5.12