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5YZI

Crystal Structure of Mouse Cytosolic Isocitrate Dehydrogenase complexed with Cadmium

Replaces:  2CMV
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
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CD A 501
ChainResidue
AASP275
AASP279
BASP252

site_idAC2
Number of Residues26
Detailsbinding site for residue NAP A 502
ChainResidue
AHIS309
AGLY310
ATHR311
AVAL312
ATHR313
AARG314
AHIS315
ATHR327
AASN328
AHOH603
AHOH605
AHOH611
AHOH612
AHOH636
AHOH643
AHOH656
BASP253
BGLN257
BLYS260
BHOH626
ALYS72
ATHR75
ATHR77
AARG82
AASN96
AALA307

site_idAC3
Number of Residues4
Detailsbinding site for residue CD B 501
ChainResidue
AASP252
BASP275
BASP279
BALA308

site_idAC4
Number of Residues3
Detailsbinding site for residue CD B 502
ChainResidue
BCYS245
BGLU247
BHOH638

site_idAC5
Number of Residues19
Detailsbinding site for residue NAP B 503
ChainResidue
AASP253
ALYS260
BLYS72
BALA74
BTHR75
BILE76
BTHR77
BASN96
BLEU288
BGLU306
BALA307
BHIS309
BGLY310
BTHR311
BVAL312
BTHR313
BARG314
BHIS315
BASN328

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 Residues20
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 Residues18
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 Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29923039","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5YZI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29923039","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"29923039","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Critical for catalysis","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O75874","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23576753","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O75874","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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