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6KDE

Crystal structure of the alpha beta heterodimer of human IDH3 in complex with Ca(2+)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004449molecular_functionisocitrate dehydrogenase (NAD+) activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005975biological_processcarbohydrate metabolic process
A0006099biological_processtricarboxylic acid cycle
A0006102biological_processisocitrate metabolic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0045242cellular_componentisocitrate dehydrogenase complex (NAD+)
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
B0000287molecular_functionmagnesium ion binding
B0006099biological_processtricarboxylic acid cycle
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0051287molecular_functionNAD binding
C0000287molecular_functionmagnesium ion binding
C0004449molecular_functionisocitrate dehydrogenase (NAD+) activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0005975biological_processcarbohydrate metabolic process
C0006099biological_processtricarboxylic acid cycle
C0006102biological_processisocitrate metabolic process
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0045242cellular_componentisocitrate dehydrogenase complex (NAD+)
C0046872molecular_functionmetal ion binding
C0051287molecular_functionNAD binding
D0000287molecular_functionmagnesium ion binding
D0006099biological_processtricarboxylic acid cycle
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CA A 401
ChainResidue
AASP230
AASP234
BASP217

site_idAC2
Number of Residues3
Detailsbinding site for residue CA C 401
ChainResidue
CASP230
CASP234
DASP217

Functional Information from PROSITE/UniProt
site_idPS00470
Number of Residues20
DetailsIDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLYGDIlSDlcAgli.GGLGV
ChainResidueDetails
AASN226-VAL245
BASN237-VAL256

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS165
CASP206
CASP230
CASP234
DLYS165
AARG119
AASP206
AASP230
AASP234
CARG88
CARG98
CARG119

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Critical for catalysis => ECO:0000269|PubMed:28098230, ECO:0000269|PubMed:28139779
ChainResidueDetails
ATYR126
CTYR126

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Critical for catalysis => ECO:0000269|PubMed:28098230
ChainResidueDetails
ALYS173
CLYS173

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9D6R2
ChainResidueDetails
ALYS50
ALYS323
CLYS50
CLYS323

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9D6R2
ChainResidueDetails
ATHR74
CTHR74

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9D6R2
ChainResidueDetails
ALYS196
CLYS196

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9D6R2
ChainResidueDetails
ALYS316
CLYS316

222624

PDB entries from 2024-07-17

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