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2QFV

Crystal structure of Saccharomyces cerevesiae mitochondrial NADP(+)-dependent isocitrate dehydrogenase in complex with NADP(+)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005777cellular_componentperoxisome
A0006097biological_processglyoxylate cycle
A0006099biological_processtricarboxylic acid cycle
A0006102biological_processisocitrate metabolic process
A0006537biological_processglutamate biosynthetic process
A0006739biological_processNADP+ metabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0042645cellular_componentmitochondrial nucleoid
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
B0000287molecular_functionmagnesium ion binding
B0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005777cellular_componentperoxisome
B0006097biological_processglyoxylate cycle
B0006099biological_processtricarboxylic acid cycle
B0006102biological_processisocitrate metabolic process
B0006537biological_processglutamate biosynthetic process
B0006739biological_processNADP+ metabolic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0042645cellular_componentmitochondrial nucleoid
B0046872molecular_functionmetal ion binding
B0051287molecular_functionNAD binding
C0000287molecular_functionmagnesium ion binding
C0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
C0005515molecular_functionprotein binding
C0005739cellular_componentmitochondrion
C0005777cellular_componentperoxisome
C0006097biological_processglyoxylate cycle
C0006099biological_processtricarboxylic acid cycle
C0006102biological_processisocitrate metabolic process
C0006537biological_processglutamate biosynthetic process
C0006739biological_processNADP+ metabolic process
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0042645cellular_componentmitochondrial nucleoid
C0046872molecular_functionmetal ion binding
C0051287molecular_functionNAD binding
D0000287molecular_functionmagnesium ion binding
D0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
D0005515molecular_functionprotein binding
D0005739cellular_componentmitochondrion
D0005777cellular_componentperoxisome
D0006097biological_processglyoxylate cycle
D0006099biological_processtricarboxylic acid cycle
D0006102biological_processisocitrate metabolic process
D0006537biological_processglutamate biosynthetic process
D0006739biological_processNADP+ metabolic process
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0042645cellular_componentmitochondrial nucleoid
D0046872molecular_functionmetal ion binding
D0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAP A 1001
ChainResidue
ALYS73
AGLY312
ATHR313
ATHR315
AARG316
AHIS317
AASN330
AHOH1007
AHOH1061
AHOH1075
AHOH1145
AALA75
AHOH1204
DGLN59
ATHR76
AILE77
ATHR78
AARG83
AASN97
AGLU308
AHIS311

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NAP B 1002
ChainResidue
BLYS73
BALA75
BTHR76
BILE77
BTHR78
BASN97
BGLU308
BHIS311
BGLY312
BTHR313
BARG316
BHIS317
BASN330
BHOH1014
BHOH1067
BHOH1181

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NAP C 1003
ChainResidue
CLYS73
CALA75
CTHR76
CILE77
CTHR78
CARG83
CASN97
CGLU308
CHIS311
CGLY312
CTHR313
CTHR315
CARG316
CHIS317
CTHR329
CASN330
CHOH1033
CHOH1053
CHOH1154
CHOH1208

site_idAC4
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAP D 1004
ChainResidue
AGLN59
DLYS73
DALA75
DTHR76
DILE77
DTHR78
DARG83
DASN97
DGLU308
DHIS311
DGLY312
DTHR313
DTHR315
DARG316
DHIS317
DTHR329
DASN330
DHOH1029
DHOH1030
DHOH1080
DHOH1161

Functional Information from PROSITE/UniProt
site_idPS00470
Number of Residues20
DetailsIDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NYDGDVqSDivAqgf.GSLGL
ChainResidueDetails
AASN273-LEU292

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues84
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsSite: {"description":"Critical for catalysis","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
AVAL156

site_idCSA10
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
BTHR163

site_idCSA11
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
CTHR163

site_idCSA12
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
DTHR163

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
BVAL156

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
CVAL156

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
DVAL156

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
AASP254
ALYS214

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
BASP254
BLYS214

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
CASP254
CLYS214

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
DASP254
DLYS214

site_idCSA9
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
ATHR163

247536

PDB entries from 2026-01-14

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