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5SVO

Structure of IDH2 mutant R140Q

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
A0006741biological_processNADP+ biosynthetic 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
A0060253biological_processnegative regulation of glial cell proliferation
A0070062cellular_componentextracellular exosome
A1903976biological_processnegative regulation of glial cell migration
A1904465biological_processnegative regulation of matrix metallopeptidase secretion
B0000287molecular_functionmagnesium ion binding
B0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005777cellular_componentperoxisome
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006097biological_processglyoxylate cycle
B0006099biological_processtricarboxylic acid cycle
B0006102biological_processisocitrate metabolic process
B0006103biological_process2-oxoglutarate metabolic process
B0006739biological_processNADP+ metabolic process
B0006741biological_processNADP+ biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0046872molecular_functionmetal ion binding
B0051287molecular_functionNAD binding
B0060253biological_processnegative regulation of glial cell proliferation
B0070062cellular_componentextracellular exosome
B1903976biological_processnegative regulation of glial cell migration
B1904465biological_processnegative regulation of matrix metallopeptidase secretion
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue NAP A 501
ChainResidue
ALYS112
AVAL351
ATHR352
AARG353
AHIS354
ATHR366
AASN367
AHOH630
AHOH641
AHOH647
AHOH670
AALA114
AHOH673
AHOH742
AHOH749
ATHR115
ATHR117
AARG122
AASN136
AHIS348
AGLY349
ATHR350

site_idAC2
Number of Residues6
Detailsbinding site for residue EPE A 502
ChainResidue
AHIS233
AGLN237
AHIS273
ATYR274
APRO337
AHOH612

site_idAC3
Number of Residues17
Detailsbinding site for residue NAP B 501
ChainResidue
BLYS112
BALA114
BTHR115
BTHR117
BASN136
BGLU345
BHIS348
BGLY349
BTHR350
BVAL351
BTHR352
BARG353
BHIS354
BASN367
BHOH626
BHOH645
BHOH658

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 Residues19
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O75874","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P33198","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsSite: {"description":"Critical for catalysis","evidences":[{"source":"UniProtKB","id":"P33198","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P54071","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues12
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues16
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P54071","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22416140","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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