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PDB code:

Information on SUBCLASS 4.1.2

Subclass Accession number: 168 Subclass: 4.1.2 Type: HH alpha-alpha DB: ArchDB-KI

Number of loops: 3 Average sequence ID (%) : 22.2 +/- 5.8 Average RMSD (Å) : 0.74 +/- 0.35 Consensus geometry d (Å): 11 delta (°): 45-90 theta (°): 135-180 rho (°): 180-225

Loops included in this Subclass

Loop	PDB	Chain	Start	End	Sequence	Sec Struct	Ramachandran
1b7b_A_251	1b7b	A	251	277	VAELEEYKQAGHFAPGSMLPKIEAAIQ	HHHHHHHHHTT-S-TTTHHHHHHHHHH	aaaaaaaaaalaxpaaaaaaaaaaaaa
1e19_A_257	1e19	A	257	283	VEELRKYYEEGHFKAGSMGPKVLAAIR	HHHHHHHHHTT-S-TTTHHHHHHHHHH	aaaaaaaaaavabpaaIaaaaaaaaaa
1kkh_A_238	1kkh	A	246	272	TKNHELLKKLNISTPKLDRIVDIGNRF	HHHHHHHHTTT---HHHHHHHHHHHHH	aaaaaaaaaalabbaaaaaaaaaaaaa

PDB ligands within a cut-off distance of 6 Å in this subclass

Loop	PDB	Chain	Ligands	Residue
1e19_A_257	1e19	A	ADPADENOSINE-5'-DIPHOSPHATE	H - 268
1e19_A_257	1e19	A	ADPADENOSINE-5'-DIPHOSPHATE	F - 269
1e19_A_257	1e19	A	ADPADENOSINE-5'-DIPHOSPHATE	K - 270
1e19_A_257	1e19	A	ADPADENOSINE-5'-DIPHOSPHATE	G - 272
1e19_A_257	1e19	A	MGMAGNESIUM ION	G - 272
1e19_A_257	1e19	A	ADPADENOSINE-5'-DIPHOSPHATE	S - 273
1e19_A_257	1e19	A	MGMAGNESIUM ION	S - 273
1e19_A_257	1e19	A	ADPADENOSINE-5'-DIPHOSPHATE	M - 274
1e19_A_257	1e19	A	ADPADENOSINE-5'-DIPHOSPHATE	G - 275
1e19_A_257	1e19	A	ADPADENOSINE-5'-DIPHOSPHATE	K - 277
1e19_A_257	1e19	A	MGMAGNESIUM ION	K - 277

Bibliographic annotations

Loop	PDB	Chain	Annotation	Residue
1e19_A_257	1e19   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;463,2000	A	REGULATORY ADP BINDING RESIDUE	H - 268
1e19_A_257	1e19   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;463,2000	A	REGULATORY ADP BINDING RESIDUE	K - 270
1e19_A_257	1e19   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;463,2000	A	Mg ION BINDING RESIDUE	G - 272
1e19_A_257	1e19   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;463,2000	A	REGULATORY ADP BINDING RESIDUE	G - 272
1e19_A_257	1e19   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;463,2000	A	Mg ION BINDING RESIDUE	S - 273
1e19_A_257	1e19   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;463,2000	A	REGULATORY ADP BINDING RESIDUE	M - 274
1e19_A_257	1e19   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;463,2000	A	CATALYTIC RESIDUE	K - 277

Clusters included in this Subclass

CLUSTER: HH.7.3

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