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6B0Z

IDH1 R132H mutant in complex with IDH305

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
D0000287molecular_functionmagnesium ion binding
D0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005777cellular_componentperoxisome
D0005782cellular_componentperoxisomal matrix
D0005829cellular_componentcytosol
D0006097biological_processglyoxylate cycle
D0006099biological_processtricarboxylic acid cycle
D0006102biological_processisocitrate metabolic process
D0006103biological_process2-oxoglutarate metabolic process
D0006739biological_processNADP metabolic process
D0006749biological_processglutathione metabolic process
D0006979biological_processresponse to oxidative stress
D0008585biological_processfemale gonad development
D0014070biological_processresponse to organic cyclic compound
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0034774cellular_componentsecretory granule lumen
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
D0045296molecular_functioncadherin binding
D0046872molecular_functionmetal ion binding
D0048545biological_processresponse to steroid hormone
D0050661molecular_functionNADP binding
D0051287molecular_functionNAD binding
D0060696biological_processregulation of phospholipid catabolic process
D0070062cellular_componentextracellular exosome
D0071071biological_processregulation of phospholipid biosynthetic process
D1904724cellular_componenttertiary granule lumen
D1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue NDP A 501
ChainResidue
ALYS72
ATHR311
AVAL312
ATHR313
AARG314
AHIS315
ATHR327
AASN328
AFLC503
AHOH601
AHOH613
AALA74
AHOH660
AHOH702
AHOH729
ATHR75
ATHR77
AARG82
AASN96
ALEU288
AHIS309
AGLY310

site_idAC2
Number of Residues15
Detailsbinding site for residue C81 A 502
ChainResidue
AARG109
AALA111
AARG119
ALEU120
ATRP124
AILE128
AILE130
AVAL255
AMET259
ASER278
AALA282
ATYR285
ASER287
AMET291
AC81504

site_idAC3
Number of Residues5
Detailsbinding site for residue FLC A 503
ChainResidue
ATHR77
ASER94
AASN96
AARG100
ANDP501

site_idAC4
Number of Residues13
Detailsbinding site for residue C81 A 504
ChainResidue
ALEU120
AHIS132
AILE251
ACYS269
AASN271
AGLN277
ASER278
AVAL281
AC81502
CLEU120
CGLN277
CVAL281
CC81502

site_idAC5
Number of Residues16
Detailsbinding site for residue NDP C 501
ChainResidue
CLYS72
CTHR75
CTHR77
CARG82
CASN96
CLEU288
CGLU306
CHIS309
CGLY310
CTHR311
CVAL312
CTHR313
CARG314
CHIS315
CASN328
CFLC503

site_idAC6
Number of Residues13
Detailsbinding site for residue C81 C 502
ChainResidue
AC81504
CARG109
CALA111
CARG119
CLEU120
CILE128
CVAL255
CTYR272
CGLN277
CSER278
CTYR285
CSER287
CMET291

site_idAC7
Number of Residues5
Detailsbinding site for residue FLC C 503
ChainResidue
CTHR77
CSER94
CASN96
CARG100
CNDP501

site_idAC8
Number of Residues27
Detailsbinding site for residue NDP B 501
ChainResidue
BGLY310
BTHR311
BVAL312
BTHR313
BARG314
BHIS315
BASN328
BFLC503
BHOH605
BHOH609
BHOH612
BHOH634
BHOH701
BHOH716
BHOH742
BHOH745
DLYS260
BLYS72
BALA74
BTHR75
BTHR77
BARG82
BASN96
BGLN283
BLEU288
BGLU306
BHIS309

site_idAC9
Number of Residues14
Detailsbinding site for residue C81 B 502
ChainResidue
BARG109
BALA111
BILE113
BARG119
BLEU120
BTRP124
BILE128
BILE130
BVAL255
BGLN277
BSER278
BVAL281
BSER287
DC81504

site_idAD1
Number of Residues6
Detailsbinding site for residue FLC B 503
ChainResidue
BTHR77
BSER94
BASN96
BARG100
BNDP501
BHOH621

site_idAD2
Number of Residues18
Detailsbinding site for residue NDP D 501
ChainResidue
DLYS72
DALA74
DTHR75
DTHR77
DARG82
DASN96
DLEU288
DGLU306
DHIS309
DGLY310
DTHR311
DVAL312
DTHR313
DARG314
DHIS315
DTHR327
DASN328
DFLC503

site_idAD3
Number of Residues15
Detailsbinding site for residue C81 D 502
ChainResidue
DARG109
DALA111
DILE113
DARG119
DLEU120
DTRP124
DILE128
DILE130
DVAL255
DMET259
DALA282
DTYR285
DSER287
DMET291
DC81504

site_idAD4
Number of Residues4
Detailsbinding site for residue FLC D 503
ChainResidue
DTHR77
DSER94
DASN96
DNDP501

site_idAD5
Number of Residues11
Detailsbinding site for residue C81 D 504
ChainResidue
BLEU120
BGLN277
BVAL281
BC81502
DLEU120
DHIS132
DCYS269
DGLN277
DSER278
DVAL281
DC81502

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 Residues12
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
BASN328
DTHR75
DGLY310
DASN328
ATHR75
AGLY310
AASN328
CTHR75
CGLY310
CASN328
BTHR75
BGLY310

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: in other chain => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L
ChainResidueDetails
CTHR77
CSER94
CARG109
CHIS132
BTHR77
BSER94
BARG109
BHIS132
DTHR77
DSER94
DARG109
DHIS132
ATHR77
ASER94
AARG109
AHIS132

site_idSWS_FT_FI3
Number of Residues4
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
CARG82
BARG82
DARG82

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L
ChainResidueDetails
ALYS212
CLYS212
BLYS212
DLYS212

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:15173171, ECO:0000305|PubMed:19935646, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM
ChainResidueDetails
CASP252
DASP252
AASP252
BASP252

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM
ChainResidueDetails
ALYS260
CLYS260
BLYS260
DLYS260

site_idSWS_FT_FI7
Number of Residues8
DetailsBINDING: in other chain => ECO:0000305|PubMed:15173171, ECO:0000305|PubMed:19935646, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM
ChainResidueDetails
BASP275
BASP279
DASP275
DASP279
AASP275
CASP279
AASP279
CASP275

site_idSWS_FT_FI8
Number of Residues8
DetailsSITE: Critical for catalysis
ChainResidueDetails
BTYR139
BLYS212
DTYR139
DLYS212
ATYR139
ALYS212
CTYR139
CLYS212

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:22814378
ChainResidueDetails
ASER2
CSER2
BSER2
DSER2

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ATYR42
DTYR42
CTYR42
BTYR42

site_idSWS_FT_FI11
Number of Residues16
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O88844
ChainResidueDetails
CLYS81
CLYS224
CLYS233
CLYS243
BLYS81
BLYS224
BLYS233
BLYS243
DLYS81
DLYS224
DLYS233
DLYS243
ALYS81
ALYS224
ALYS233
ALYS243

site_idSWS_FT_FI12
Number of Residues8
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:O88844
ChainResidueDetails
ALYS126
ALYS400
CLYS126
CLYS400
BLYS126
BLYS400
DLYS126
DLYS400

site_idSWS_FT_FI13
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS321
CLYS321
BLYS321
DLYS321

site_idSWS_FT_FI14
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O88844
ChainResidueDetails
ASER389
CSER389
BSER389
DSER389

219869

PDB entries from 2024-05-15

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