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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8W49

mouse isocitrate dehydrogenase with isocitrate and magnesium

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
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
A0006740biological_processNADPH regeneration
A0006749biological_processglutathione metabolic process
A0006979biological_processresponse to oxidative stress
A0008585biological_processfemale gonad development
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0048545biological_processresponse to steroid hormone
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
A0060696biological_processregulation of phospholipid catabolic process
A0071071biological_processregulation of phospholipid biosynthetic process
B0000287molecular_functionmagnesium ion binding
B0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
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
B0006740biological_processNADPH regeneration
B0006749biological_processglutathione metabolic process
B0006979biological_processresponse to oxidative stress
B0008585biological_processfemale gonad development
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0048545biological_processresponse to steroid hormone
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
B0060696biological_processregulation of phospholipid catabolic process
B0071071biological_processregulation of phospholipid biosynthetic process
C0000287molecular_functionmagnesium ion binding
C0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
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
C0006740biological_processNADPH regeneration
C0006749biological_processglutathione metabolic process
C0006979biological_processresponse to oxidative stress
C0008585biological_processfemale gonad development
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
C0046872molecular_functionmetal ion binding
C0048545biological_processresponse to steroid hormone
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
C0060696biological_processregulation of phospholipid catabolic process
C0071071biological_processregulation of phospholipid biosynthetic process
D0000287molecular_functionmagnesium ion binding
D0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
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
D0006740biological_processNADPH regeneration
D0006749biological_processglutathione metabolic process
D0006979biological_processresponse to oxidative stress
D0008585biological_processfemale gonad development
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
D0046872molecular_functionmetal ion binding
D0048545biological_processresponse to steroid hormone
D0050661molecular_functionNADP binding
D0051287molecular_functionNAD binding
D0060696biological_processregulation of phospholipid catabolic process
D0071071biological_processregulation of phospholipid biosynthetic process
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 Residues40
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29923039","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5YZH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5YZI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues36
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"29923039","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5YZI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29923039","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5YZI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29923039","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"29923039","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues8
DetailsSite: {"description":"Critical for catalysis","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O75874","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues16
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23576753","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues8
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O75874","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"UniProtKB","id":"O75874","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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