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8T7D

Crystal structure of wild type IDH1 bound to compound 1

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

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: in other chain => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L
ChainResidueDetails
ATHR77
CSER94
CARG109
CARG132
DTHR77
DSER94
DARG109
DARG132
ASER94
AARG109
AARG132
BTHR77
BSER94
BARG109
BARG132
CTHR77

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
BARG82
CARG82
DARG82

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L
ChainResidueDetails
ALYS212
BLYS212
CLYS212
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
AASP252
BASP252
CASP252
DASP252

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
BLYS260
CLYS260
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
AASP275
AASP279
BASP275
BASP279
CASP275
CASP279
DASP275
DASP279

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

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

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

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

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

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

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

224201

PDB entries from 2024-08-28

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