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3INM

Crystal structure of human cytosolic NADP(+)-dependent isocitrate dehydrogenase R132H mutant in complex with NADPH, ALPHA-KETOGLUTARATE and CALCIUM(2+)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005777cellular_componentperoxisome
A0005782cellular_componentperoxisomal matrix
A0005829cellular_componentcytosol
A0006097biological_processglyoxylate cycle
A0006099biological_processtricarboxylic acid cycle
A0006102biological_processisocitrate metabolic process
A0006103biological_process2-oxoglutarate metabolic process
A0006739biological_processNADP metabolic process
A0006749biological_processglutathione metabolic process
A0006979biological_processresponse to oxidative stress
A0008585biological_processfemale gonad development
A0014070biological_processresponse to organic cyclic compound
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0034774cellular_componentsecretory granule lumen
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0045296molecular_functioncadherin binding
A0046872molecular_functionmetal ion binding
A0048545biological_processresponse to steroid hormone
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
A0060696biological_processregulation of phospholipid catabolic process
A0070062cellular_componentextracellular exosome
A0071071biological_processregulation of phospholipid biosynthetic process
A1904724cellular_componenttertiary granule lumen
A1904813cellular_componentficolin-1-rich granule lumen
B0000287molecular_functionmagnesium ion binding
B0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005777cellular_componentperoxisome
B0005782cellular_componentperoxisomal matrix
B0005829cellular_componentcytosol
B0006097biological_processglyoxylate cycle
B0006099biological_processtricarboxylic acid cycle
B0006102biological_processisocitrate metabolic process
B0006103biological_process2-oxoglutarate metabolic process
B0006739biological_processNADP metabolic process
B0006749biological_processglutathione metabolic process
B0006979biological_processresponse to oxidative stress
B0008585biological_processfemale gonad development
B0014070biological_processresponse to organic cyclic compound
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0034774cellular_componentsecretory granule lumen
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0045296molecular_functioncadherin binding
B0046872molecular_functionmetal ion binding
B0048545biological_processresponse to steroid hormone
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
B0060696biological_processregulation of phospholipid catabolic process
B0070062cellular_componentextracellular exosome
B0071071biological_processregulation of phospholipid biosynthetic process
B1904724cellular_componenttertiary granule lumen
B1904813cellular_componentficolin-1-rich granule lumen
C0000287molecular_functionmagnesium ion binding
C0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005777cellular_componentperoxisome
C0005782cellular_componentperoxisomal matrix
C0005829cellular_componentcytosol
C0006097biological_processglyoxylate cycle
C0006099biological_processtricarboxylic acid cycle
C0006102biological_processisocitrate metabolic process
C0006103biological_process2-oxoglutarate metabolic process
C0006739biological_processNADP metabolic process
C0006749biological_processglutathione metabolic process
C0006979biological_processresponse to oxidative stress
C0008585biological_processfemale gonad development
C0014070biological_processresponse to organic cyclic compound
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0034774cellular_componentsecretory granule lumen
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
C0045296molecular_functioncadherin binding
C0046872molecular_functionmetal ion binding
C0048545biological_processresponse to steroid hormone
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
C0060696biological_processregulation of phospholipid catabolic process
C0070062cellular_componentextracellular exosome
C0071071biological_processregulation of phospholipid biosynthetic process
C1904724cellular_componenttertiary granule lumen
C1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NDP A 501
ChainResidue
ALYS72
ATHR311
AVAL312
ATHR313
AARG314
AHIS315
ATHR327
AASN328
AHOH428
AHOH429
AHOH431
AALA74
AHOH433
AHOH434
AHOH435
AHOH437
AHOH438
AAKG511
ANA522
BLEU250
BASP253
BGLN257
ATHR75
BLYS260
BHOH426
ATHR77
AARG82
AASN96
ALEU288
AHIS309
AGLY310

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AKG A 511
ChainResidue
ATHR77
ASER94
AASN96
AARG100
AARG109
ATYR139
AASP275
AHOH431
ANDP501
ACA521
BLYS212
BILE215
BASP252

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 521
ChainResidue
AASP275
AASP279
AHOH426
AHOH427
AAKG511
BASP252

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA A 522
ChainResidue
ANDP501

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 531
ChainResidue
AGLN323
AGLU324
ATHR325
AASN393
ATHR394
APHE395

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 532
ChainResidue
APHE108
AARG109
AGLU110
AMET199
ATHR292

site_idAC7
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NDP B 501
ChainResidue
AASP253
AGLN257
ALYS260
BLYS72
BALA74
BTHR75
BTHR77
BARG82
BASN96
BALA308
BHIS309
BGLY310
BTHR311
BVAL312
BARG314
BHIS315
BTHR327
BASN328
BHOH429
BHOH430
BHOH431
BHOH433
BHOH434
BHOH435
BHOH436
BAKG511
BNA522

site_idAC8
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AKG B 511
ChainResidue
BNDP501
BCA521
AASP252
BTHR77
BSER94
BASN96
BARG100
BARG109
BTYR139
BASP275
BALA308
BHOH431

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 521
ChainResidue
AASP252
BASP275
BASP279
BHOH427
BHOH428
BAKG511

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NA B 522
ChainResidue
BNDP501

site_idBC2
Number of Residues30
DetailsBINDING SITE FOR RESIDUE NDP C 501
ChainResidue
CALA74
CTHR75
CILE76
CTHR77
CARG82
CASN96
CLEU250
CASP253
CGLN257
CLYS260
CLEU288
CALA307
CALA308
CHIS309
CGLY310
CTHR311
CVAL312
CTHR313
CARG314
CHIS315
CASN328
CHOH428
CHOH429
CHOH433
CHOH434
CHOH435
CHOH436
CHOH438
CAKG511
CNA522

site_idBC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AKG C 511
ChainResidue
CTHR77
CSER94
CASN96
CARG100
CARG109
CTYR139
CLYS212
CILE215
CASP252
CASP275
CHOH431
CNDP501
CCA521

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 521
ChainResidue
CASP252
CASP275
CASP279
CHOH426
CHOH427
CAKG511

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA C 522
ChainResidue
CARG314
CNDP501

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 532
ChainResidue
CPHE108
CGLU110
CILE129
CMET199
CLYS203
CTHR292

Functional Information from PROSITE/UniProt
site_idPS00470
Number of Residues20
DetailsIDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NYDGDVqSDsvAqgy.GSLGM
ChainResidueDetails
AASN271-MET290

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T09, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM, ECO:0007744|PDB:3MAP, ECO:0007744|PDB:3MAR, ECO:0007744|PDB:3MAS, ECO:0007744|PDB:4I3K, ECO:0007744|PDB:4I3L, ECO:0007744|PDB:4KZO, ECO:0007744|PDB:4L03, ECO:0007744|PDB:4L04, ECO:0007744|PDB:4L06, ECO:0007744|PDB:4UMX, ECO:0007744|PDB:4UMY, ECO:0007744|PDB:4XRX, ECO:0007744|PDB:4XS3, ECO:0007744|PDB:5DE1, ECO:0007744|PDB:5L57, ECO:0007744|PDB:5L58, ECO:0007744|PDB:5LGE, ECO:0007744|PDB:5SUN, ECO:0007744|PDB:5SVF, ECO:0007744|PDB:5TQH
ChainResidueDetails
ATHR75
AGLY310
AASN328
BTHR75
BGLY310
BASN328
CTHR75
CGLY310
CASN328

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: in other chain => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L
ChainResidueDetails
ATHR77
CSER94
CARG109
CHIS132
ASER94
AARG109
AHIS132
BTHR77
BSER94
BARG109
BHIS132
CTHR77

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T09, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM, ECO:0007744|PDB:3MAP, ECO:0007744|PDB:3MAR, ECO:0007744|PDB:3MAS, ECO:0007744|PDB:4I3K, ECO:0007744|PDB:4I3L, ECO:0007744|PDB:4KZO, ECO:0007744|PDB:4L03, ECO:0007744|PDB:4L04, ECO:0007744|PDB:4L06, ECO:0007744|PDB:4UMX, ECO:0007744|PDB:4UMY, ECO:0007744|PDB:4XRX, ECO:0007744|PDB:4XS3, ECO:0007744|PDB:5DE1, ECO:0007744|PDB:5L57, ECO:0007744|PDB:5LGE, ECO:0007744|PDB:5SUN, ECO:0007744|PDB:5SVF, ECO:0007744|PDB:5TQH
ChainResidueDetails
AARG82
BARG82
CARG82

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L
ChainResidueDetails
ALYS212
BLYS212
CLYS212

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:15173171, ECO:0000305|PubMed:19935646, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM
ChainResidueDetails
AASP252
BASP252
CASP252

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM
ChainResidueDetails
ALYS260
BLYS260
CLYS260

site_idSWS_FT_FI7
Number of Residues6
DetailsBINDING: in other chain => ECO:0000305|PubMed:15173171, ECO:0000305|PubMed:19935646, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM
ChainResidueDetails
AASP275
AASP279
BASP275
BASP279
CASP275
CASP279

site_idSWS_FT_FI8
Number of Residues6
DetailsSITE: Critical for catalysis
ChainResidueDetails
ATYR139
ALYS212
BTYR139
BLYS212
CTYR139
CLYS212

site_idSWS_FT_FI9
Number of Residues3
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:22814378
ChainResidueDetails
ASER2
BSER2
CSER2

site_idSWS_FT_FI10
Number of Residues3
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATYR42
BTYR42
CTYR42

site_idSWS_FT_FI11
Number of Residues12
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O88844
ChainResidueDetails
ALYS81
CLYS224
CLYS233
CLYS243
ALYS224
ALYS233
ALYS243
BLYS81
BLYS224
BLYS233
BLYS243
CLYS81

site_idSWS_FT_FI12
Number of Residues6
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:O88844
ChainResidueDetails
ALYS126
ALYS400
BLYS126
BLYS400
CLYS126
CLYS400

site_idSWS_FT_FI13
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS321
BLYS321
CLYS321

site_idSWS_FT_FI14
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O88844
ChainResidueDetails
ASER389
BSER389
CSER389

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
ATHR155

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
BTHR155

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
CTHR155

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
ALYS212
AASP252

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
BLYS212
BASP252

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a05
ChainResidueDetails
CLYS212
CASP252

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PDB entries from 2024-11-06

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