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36UI

Crystal Structure of IDH2 (R140Q) in complex with covalent inhibitor LY3410738

This is a non-PDB format compatible entry.
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
A0006099biological_processtricarboxylic acid cycle
A0006102biological_processisocitrate metabolic process
A0006103biological_process2-oxoglutarate metabolic process
A0006739biological_processNADP+ metabolic process
A0006741biological_processNADP+ biosynthetic process
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
B0006099biological_processtricarboxylic acid cycle
B0006102biological_processisocitrate metabolic process
B0006103biological_process2-oxoglutarate metabolic process
B0006739biological_processNADP+ metabolic process
B0006741biological_processNADP+ biosynthetic process
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 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 Residues20
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"O75874","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues21
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P33198","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
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 Residues15
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

259351

PDB entries from 2026-09-09

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