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1HQS

CRYSTAL STRUCTURE OF ISOCITRATE DEHYDROGENASE FROM BACILLUS SUBTILIS

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
A0005515molecular_functionprotein binding
A0006097biological_processglyoxylate cycle
A0006099biological_processtricarboxylic acid cycle
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
B0000287molecular_functionmagnesium ion binding
B0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
B0005515molecular_functionprotein binding
B0006097biological_processglyoxylate cycle
B0006099biological_processtricarboxylic acid cycle
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0046872molecular_functionmetal ion binding
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CIT A 425
ChainResidue
ATHR96
AHOH1501
BLYS221
BASN223
BILE224
ASER104
AASN106
AARG110
AARG144
ATYR151
ATHR344
AHIS345
AHOH1438

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CIT B 825
ChainResidue
ALYS221
AASN223
AILE224
APGR907
BTHR96
BSER104
BASN106
BARG110
BARG144
BTYR151
BASP311

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PGO A 901
ChainResidue
APRO121
AVAL122
AARG123
APHE125
AVAL321
AILE326
APRO328
APGO902

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PGO A 902
ChainResidue
AARG123
APGO901
AHOH1369

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGO B 903
ChainResidue
AHOH1105
BARG134
BASP137
BTHR295
BHOH1592

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGO B 904
ChainResidue
BTRP251
BTYR254
BGLN270
BHOH1463

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGO B 905
ChainResidue
BPRO121
BARG123
BHOH1338
BHOH1489
BHOH1579
BHOH1589

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGR A 906
ChainResidue
ATYR237
ATRP251
AALA252
AASP255
AASP283
AHOH1215

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGR A 907
ChainResidue
ALYS221
AASN223
AILE285
AASP287
AILE288
BCIT825

Functional Information from PROSITE/UniProt
site_idPS00470
Number of Residues20
DetailsIDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLNGDYiSDalAaqv.GGIGI
ChainResidueDetails
AASN307-ILE326

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATHR95
BASP311
BHIS345
BASN358
BTYR397
BARG401
AARG120
AASP311
AHIS345
AASN358
ATYR397
AARG401
BTHR95
BARG120

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING:
ChainResidueDetails
ATHR96
BARG144
ASER104
AASN106
AARG110
AARG144
BTHR96
BSER104
BASN106
BARG110

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Critical for catalysis => ECO:0000250
ChainResidueDetails
ATYR151
ALYS221
BTYR151
BLYS221

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
ALYS221
AASP287
BTYR151

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
ATYR151
BLYS221
BASP287

224004

PDB entries from 2024-08-21

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