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Information on SUBCLASS 3.2.1
Subclass Accession number: 121
Subclass: 3.2.1
Type: HE alpha-beta
DB: ArchDB-KI
Number of loops: 8

Average sequence ID (%) : 11.8 +/- 0.6
Average RMSD (Å) : 0.86 +/- 0.39

Consensus geometry
d (Å): 9 delta (°): 90-135 theta (°): 135-180 rho (°): 45-90
Consensus Sequence: pXGXpXh
(φψ)-conformation: aagpabb
Pattern: x{GILM}x{AILV}xx{ACFGL}x{EKL}x{GN}x{DEKN}x{AIV}{AFIMWY}[ACFIL]
Conservation:-0.554-0.658-0.3860.520-0.620-0.605-0.405-0.3961.134-0.9873.096-0.4140.824-0.6660.296-0.6020.426
Loops included in this Subclass
LoopPDBChainStartEndSequenceSec StructRamachandran
1dku_A_2301dku   A233249TLAANALVENGAKEVYAHHHHHHHHHTT-SEEEEaaaaaaaaaagxabbbb
1dku_A_681dku   A7692LIMVDALKRASAKTINIHHHHHHHHHTT-SEEEEaaaaaaaaaavpabbbx
1e0t_A_1721e0t   A175191KQDLIFGCEQGVDFVAAHHHHHHHHHHT-SEEEEaaaaaaaaaavxabbxx
1e0t_A_2921e0t   A295311AGDVANAILDGTDAVMLHHHHHHHHHHT-SEEEEaaaaaaaaaagpabbxb
1e19_A_2741e19   A278294VLAAIRFIEWGGERAIIHHHHHHHHHHT-SEEEEaaaaaaaaaagxabbbb
1gc5_A_781gc5   A8298LGGILRSIKLGKAMEWFHHHHHHHHHS---EEEEaaaaaaaaaalbxbbbx
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_2741e19   A     ADPADENOSINE-5'-DIPHOSPHATE M - 274
1e19_A_2741e19   A     ADPADENOSINE-5'-DIPHOSPHATE G - 275
1e19_A_2741e19   A     ADPADENOSINE-5'-DIPHOSPHATE K - 277
1e19_A_2741e19   A     MGMAGNESIUM ION K - 277
Bibliographic annotations
LoopPDBChainAnnotationResidue
1dku_A_681dku   RefT.A.ERIKSEN,A.KADZIOLA,A.-K.BENTSEN,K.W.HARLOW,S.LARSEN. STRUCTURAL BASIS FOR THE FUNCTION OF BACILLUS SUBTILIS PHOSPHORIBOSYL-PYROPHOSPHATE SYNTHETASE  NAT.STRUCT.BIOL. v.7;303,2000AREGULATORY ADP BINDING RESIDUEA - 85
1dku_A_681dku   RefT.A.ERIKSEN,A.KADZIOLA,A.-K.BENTSEN,K.W.HARLOW,S.LARSEN. STRUCTURAL BASIS FOR THE FUNCTION OF BACILLUS SUBTILIS PHOSPHORIBOSYL-PYROPHOSPHATE SYNTHETASE  NAT.STRUCT.BIOL. v.7;303,2000AREGULATORY ADP BINDING RESIDUEA - 85
1dku_A_681dku   RefT.A.ERIKSEN,A.KADZIOLA,A.-K.BENTSEN,K.W.HARLOW,S.LARSEN. STRUCTURAL BASIS FOR THE FUNCTION OF BACILLUS SUBTILIS PHOSPHORIBOSYL-PYROPHOSPHATE SYNTHETASE  NAT.STRUCT.BIOL. v.7;303,2000AREGULATORY ADP BINDING RESIDUES - 86
1e19_A_2741e19   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 RESIDUEM - 274
1e19_A_2741e19   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 - 277

Clusters included in this Subclass
CLUSTER: HE.3.7