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2QFW

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

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
E0000287molecular_functionmagnesium ion binding
E0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
E0005515molecular_functionprotein binding
E0005739cellular_componentmitochondrion
E0005777cellular_componentperoxisome
E0006097biological_processglyoxylate cycle
E0006099biological_processtricarboxylic acid cycle
E0006102biological_processisocitrate metabolic process
E0006537biological_processglutamate biosynthetic process
E0006739biological_processNADP+ metabolic process
E0016491molecular_functionoxidoreductase activity
E0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E0042645cellular_componentmitochondrial nucleoid
E0046872molecular_functionmetal ion binding
E0051287molecular_functionNAD binding
F0000287molecular_functionmagnesium ion binding
F0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
F0005515molecular_functionprotein binding
F0005739cellular_componentmitochondrion
F0005777cellular_componentperoxisome
F0006097biological_processglyoxylate cycle
F0006099biological_processtricarboxylic acid cycle
F0006102biological_processisocitrate metabolic process
F0006537biological_processglutamate biosynthetic process
F0006739biological_processNADP+ metabolic process
F0016491molecular_functionoxidoreductase activity
F0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F0042645cellular_componentmitochondrial nucleoid
F0046872molecular_functionmetal ion binding
F0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ICT A 2101
ChainResidue
ATHR78
BASP254
ASER95
AASN97
AARG101
AARG110
AARG133
ATYR140
AASP277
BLYS214

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ICT B 2102
ChainResidue
ALYS214
AASP254
BTHR78
BSER95
BASN97
BARG101
BARG110
BARG133
BTYR140
BASP277
BHOH2305

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ICT C 2103
ChainResidue
CTHR78
CSER95
CASN97
CARG101
CARG110
CARG133
CTYR140
CASP277
CHOH2131
DLYS214
DILE217
DASP254

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ICT D 2104
ChainResidue
CHOH2195
DSER95
DASN97
DARG101
DARG110
DARG133
DASP277
DHOH2135
DHOH2139
DHOH2254

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ICT E 2105
ChainResidue
ETHR78
ESER95
EASN97
EARG101
EARG110
EARG133
ETYR140
EASP277
EHOH2108
FLYS214
FASP254
FHOH2141

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ICT F 2106
ChainResidue
EILE217
EASP254
FTHR78
FSER95
FASN97
FARG101
FARG110
FARG133
FASP277
FHOH2126

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 Residues126
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
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 Residues2
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
DASP254
DLYS214

site_idCSA11
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
EASP254
ELYS214

site_idCSA12
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
FASP254
FLYS214

site_idCSA13
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
ATHR163

site_idCSA14
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
BTHR163

site_idCSA15
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
CTHR163

site_idCSA16
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
DTHR163

site_idCSA17
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
ETHR163

site_idCSA18
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
FTHR163

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 Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
EVAL156

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
FVAL156

site_idCSA7
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
AASP254
ALYS214

site_idCSA8
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
BASP254
BLYS214

site_idCSA9
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
CASP254
CLYS214

247536

PDB entries from 2026-01-14

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