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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8VHE

Crystal Structure of Human IDH1 R132Q in Complex with NADPH-TCEP Adduct

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
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
A0034774cellular_componentsecretory granule lumen
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0045296molecular_functioncadherin binding
A0046872molecular_functionmetal ion binding
A0048545biological_processresponse to steroid hormone
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
A0060696biological_processregulation of phospholipid catabolic process
A0070062cellular_componentextracellular exosome
A0071071biological_processregulation of phospholipid biosynthetic process
A1904724cellular_componenttertiary granule lumen
A1904813cellular_componentficolin-1-rich granule lumen
B0000287molecular_functionmagnesium ion binding
B0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
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
B0034774cellular_componentsecretory granule lumen
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0045296molecular_functioncadherin binding
B0046872molecular_functionmetal ion binding
B0048545biological_processresponse to steroid hormone
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
B0060696biological_processregulation of phospholipid catabolic process
B0070062cellular_componentextracellular exosome
B0071071biological_processregulation of phospholipid biosynthetic process
B1904724cellular_componenttertiary granule lumen
B1904813cellular_componentficolin-1-rich granule lumen
C0000287molecular_functionmagnesium ion binding
C0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
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
C0034774cellular_componentsecretory granule lumen
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
C0045296molecular_functioncadherin binding
C0046872molecular_functionmetal ion binding
C0048545biological_processresponse to steroid hormone
C0050661molecular_functionNADP binding
C0051287molecular_functionNAD binding
C0060696biological_processregulation of phospholipid catabolic process
C0070062cellular_componentextracellular exosome
C0071071biological_processregulation of phospholipid biosynthetic process
C1904724cellular_componenttertiary granule lumen
C1904813cellular_componentficolin-1-rich granule lumen
D0000287molecular_functionmagnesium ion binding
D0004450molecular_functionisocitrate dehydrogenase (NADP+) activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
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
D0034774cellular_componentsecretory granule lumen
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
D0045296molecular_functioncadherin binding
D0046872molecular_functionmetal ion binding
D0048545biological_processresponse to steroid hormone
D0050661molecular_functionNADP binding
D0051287molecular_functionNAD binding
D0060696biological_processregulation of phospholipid catabolic process
D0070062cellular_componentextracellular exosome
D0071071biological_processregulation of phospholipid biosynthetic process
D1904724cellular_componenttertiary granule lumen
D1904813cellular_componentficolin-1-rich granule lumen
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 Residues32
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15173171","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19935646","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T09","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T0L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3INM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MAP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MAR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MAS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I3K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I3L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KZO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L04","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UMX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UMY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4XRX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4XS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5DE1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5L57","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5L58","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LGE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SUN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5TQH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues36
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"15173171","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T0L","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15173171","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19935646","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T09","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T0L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3INM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MAP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MAR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MAS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I3K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4I3L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4KZO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L04","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4L06","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UMX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UMY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4XRX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4XS3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5DE1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5L57","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LGE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SUN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5TQH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15173171","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T0L","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15173171","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19935646","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1T0L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3INM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15173171","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19935646","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T0L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3INM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"15173171","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19935646","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1T0L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3INM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues8
DetailsSite: {"description":"Critical for catalysis"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues16
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O88844","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues8
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"O88844","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O88844","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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