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Information on SUBCLASS 3.1.7
Subclass Accession number: 120
Subclass: 3.1.7
Type: HE alpha-beta
DB: ArchDB-KI
Number of loops: 3

Average sequence ID (%) : 26.7 +/- 7.4
Average RMSD (Å) : 0.73 +/- 0.36

Consensus geometry
d (Å): 11 delta (°): 90-135 theta (°): 135-180 rho (°): 0-45
Consensus Sequence: XhXhpXX
(φψ)-conformation: aalpabb
Pattern: [KL][DS]x[A]x[EN][KQ][EL][AL][EN][EKL][AV][DGN][AI][DK]xx[MV][AI][LT]
Conservation:-0.3410.901-1.2512.123-1.4620.9261.219-0.950-0.1940.926-1.0400.2700.225-0.1940.608-1.357-1.1460.956-0.194-0.024
Loops included in this Subclass
LoopPDBChainStartEndSequenceSec StructRamachandran
1b7b_A_2091b7b   A209228KDFASEKLAELVDADALVILHHHHHHHHHHHHT-SEEEEEaaaaaaaaaaaalxabbbbx
1b7b_A_751b7b   A90109LSNALNQELNKAGIKKQVATHHHHHHHHHHHTT---EEEEaaaaaaaaaaaavxbbxbbb
1e19_A_2151e19   A215234KDLAGEKLAEEVNADIFMILHHHHHHHHHHHTT-SEEEEEaaaaaaaaaaaalxabbbxb
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
Bibliographic annotations
LoopPDBChainAnnotationResidue
1b7b_A_751b7b   RefA.MARINA,P.M.ALZARI,J.BRAVO,M.URIARTE,B.BARCELONA,I.FITA,V.RUBIO. CARBAMATE KINASE: NEW STRUCTURAL MACHINERY FOR MAKING CARBAMOYL PHOSPHATE, THE COMMON PRECURSOR OF PYRIMIDINES AND ARGININE  PROTEIN SCI. v.8;934,1999AMONOMER-MONOMER INTERACTION RESIDUEC - 78
1b7b_A_751b7b   RefA.MARINA,P.M.ALZARI,J.BRAVO,M.URIARTE,B.BARCELONA,I.FITA,V.RUBIO. CARBAMATE KINASE: NEW STRUCTURAL MACHINERY FOR MAKING CARBAMOYL PHOSPHATE, THE COMMON PRECURSOR OF PYRIMIDINES AND ARGININE  PROTEIN SCI. v.8;934,1999AMONOMER-MONOMER INTERACTION RESIDUEM - 81
1b7b_A_751b7b   RefA.MARINA,P.M.ALZARI,J.BRAVO,M.URIARTE,B.BARCELONA,I.FITA,V.RUBIO. CARBAMATE KINASE: NEW STRUCTURAL MACHINERY FOR MAKING CARBAMOYL PHOSPHATE, THE COMMON PRECURSOR OF PYRIMIDINES AND ARGININE  PROTEIN SCI. v.8;934,1999AMONOMER-MONOMER INTERACTION RESIDUET - 109
1b7b_A_2091b7b   RefA.MARINA,P.M.ALZARI,J.BRAVO,M.URIARTE,B.BARCELONA,I.FITA,V.RUBIO. CARBAMATE KINASE: NEW STRUCTURAL MACHINERY FOR MAKING CARBAMOYL PHOSPHATE, THE COMMON PRECURSOR OF PYRIMIDINES AND ARGININE  PROTEIN SCI. v.8;934,1999ACONSERVED RESIDUED - 210
1b7b_A_2091b7b   RefA.MARINA,P.M.ALZARI,J.BRAVO,M.URIARTE,B.BARCELONA,I.FITA,V.RUBIO. CARBAMATE KINASE: NEW STRUCTURAL MACHINERY FOR MAKING CARBAMOYL PHOSPHATE, THE COMMON PRECURSOR OF PYRIMIDINES AND ARGININE  PROTEIN SCI. v.8;934,1999APUTATIVE ACTIVE SITE RESIDUED - 210
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

Clusters included in this Subclass
CLUSTER: HE.4.20