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Information on SUBCLASS 3.1.5
Subclass Accession number: 118
Subclass: 3.1.5
Type: HE alpha-beta
DB: ArchDB-KI
 Number of loops: 4

Average sequence ID (%) : 26.3 +/- 3.3
Average RMSD (Å) : 0.84 +/- 0.55

Consensus geometry
d (Å): 11 delta (°): 90-135 theta (°): 135-180 rho (°): 0-45
Consensus Sequence: phpAphh
(φψ)-conformation: aalpabb
Pattern: x{FLT}{A}{AGM}[ENR]{K}[L][AM][DE]{EL}[LTV]{DKN}[AI]{DP}{AI}[AFIL]{IMV}[FI]x
Conservation:-0.660-1.4110.412-0.7400.2530.2952.2250.3652.120-0.6760.007-0.4040.2730.540-1.028-0.572-0.5160.848-1.332
Loops included in this Subclass
LoopPDBChainStartEndSequenceSec StructRamachandran
1b7b_A_2091b7b   A210228DFASEKLAELVDADALVILHHHHHHHHHHHT-SEEEEEaaaaaaaaaaalxabbbbx
1dku_A_1781dku   A178196VTRARKLADRLKAPIAIIDHHHHHHHHHHTT--EEEEEaaaaaaaaaaalbxbbbxb
1e19_A_2151e19   A216234DLAGEKLAEEVNADIFMILHHHHHHHHHHTT-SEEEEEaaaaaaaaaaalxabbbxb
1gc5_A_3301gc5   A334352IDAMNVLMDETGIERIHFHHHHHHHHHHHH--SEEEEEaaaaaaaaaaavxabbbbb
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_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.3.11