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3MBC

Crystal structure of monomeric isocitrate dehydrogenase from Corynebacterium glutamicum in complex with NADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
A0005737cellular_componentcytoplasm
A0006097biological_processglyoxylate cycle
A0006099biological_processtricarboxylic acid cycle
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
B0005737cellular_componentcytoplasm
B0006097biological_processglyoxylate cycle
B0006099biological_processtricarboxylic acid cycle
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 739
ChainResidue
AASP346
AASP544
AASP548
AHOH1109
AHOH1110

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE NAP A 740
ChainResidue
ATRP597
AASP598
AARG645
AHOH1111
AHOH1251
AHOH1257
AHOH1302
AGLY579
AGLY580
AHIS585
AARG596

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 739
ChainResidue
BASP346
BASP544
BASP548
BHOH832
BHOH833

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P16100
ChainResidueDetails
AASN83
BASN83
BSER85
BSER130
BASN133
BARG137
BARG143
BLYS253
BTYR416
BARG543
ASER85
ASER130
AASN133
AARG137
AARG143
ALYS253
ATYR416
AARG543

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16416443, ECO:0000269|PubMed:21931217, ECO:0007744|PDB:2B0T, ECO:0007744|PDB:3MBC
ChainResidueDetails
AASP346
AASP544
AASP548
BASP346
BASP544
BASP548

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:21931217, ECO:0007744|PDB:3MBC
ChainResidueDetails
AGLY580
BARG645
AHIS585
AARG596
AASP598
AARG645
BGLY580
BHIS585
BARG596
BASP598

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PDB entries from 2025-06-11

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