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5I95

Crystal Structure of Human Mitochondrial Isocitrate Dehydrogenase R140Q Mutant Homodimer bound to NADPH and alpha-Ketoglutaric acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006097biological_processglyoxylate cycle
A0006099biological_processtricarboxylic acid cycle
A0006102biological_processisocitrate metabolic process
A0006103biological_process2-oxoglutarate metabolic process
A0006739biological_processNADP metabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues34
Detailsbinding site for residue NDP A 501
ChainResidue
ALYS112
AGLN296
ALYS299
AHIS348
AGLY349
ATHR350
AVAL351
ATHR352
AARG353
AHIS354
AASN367
AALA114
AAKG508
AHOH665
AHOH683
AHOH711
AHOH724
AHOH733
AHOH746
AHOH761
AHOH776
AHOH780
ATHR115
AHOH785
AHOH786
AHOH811
AHOH880
AHOH948
AILE116
ATHR117
AARG122
AASN136
ALEU289
AASP292

site_idAC2
Number of Residues7
Detailsbinding site for residue CA A 502
ChainResidue
AARG149
AASP291
AASP314
AASP318
AAKG508
AHOH619
AHOH658

site_idAC3
Number of Residues8
Detailsbinding site for residue GOL A 503
ChainResidue
APHE184
AVAL185
AALA186
AASP187
AARG188
APHE196
AHOH640
AHOH668

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL A 504
ChainResidue
APHE148
AGLU150
ATYR238
AARG377
AHOH629
AHOH791

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL A 505
ChainResidue
ALYS280
ALYS282
AGOL506
AHOH769

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL A 506
ChainResidue
AMET397
AGLU404
AARG451
AGOL505
AHOH617
AHOH920

site_idAC7
Number of Residues2
Detailsbinding site for residue ACT A 507
ChainResidue
ALYS413
APHE431

site_idAC8
Number of Residues16
Detailsbinding site for residue AKG A 508
ChainResidue
ATHR117
ASER134
AASN136
AARG149
AARG172
ALYS251
AILE254
AASP291
AASP314
AALA347
ANDP501
ACA502
AHOH632
AHOH658
AHOH733
AHOH822

Functional Information from PROSITE/UniProt
site_idPS00470
Number of Residues20
DetailsIDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NYDGDVqSDilAqgf.GSLGL
ChainResidueDetails
AASN310-LEU329

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O75874
ChainResidueDetails
ATHR115
AARG122
ALYS299
AGLY349
AASN367

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P33198
ChainResidueDetails
ATHR117
ASER134
AARG149
AARG172
AASP291
AASP314

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Critical for catalysis => ECO:0000250|UniProtKB:P33198
ChainResidueDetails
ATYR179
ALYS251

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P54071
ChainResidueDetails
ALYS45
ALYS48
ALYS69
ALYS199
ALYS280
ALYS400

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS67
ALYS155
ALYS263
ALYS272
ALYS275
ALYS442

site_idSWS_FT_FI6
Number of Residues8
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P54071
ChainResidueDetails
ALYS80
ALYS106
ALYS166
ALYS180
ALYS193
ALYS256
ALYS282
ALYS384

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:22416140
ChainResidueDetails
ALYS413

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數據於2024-09-18公開中

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