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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7ZYT

Crystal structure of the I318T pathogenic variant of the human dihydrolipoamide dehydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0001669cellular_componentacrosomal vesicle
A0004148molecular_functiondihydrolipoyl dehydrogenase (NADH) activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005929cellular_componentcilium
A0006086biological_processpyruvate decarboxylation to acetyl-CoA
A0006103biological_process2-oxoglutarate metabolic process
A0006120biological_processmitochondrial electron transport, NADH to ubiquinone
A0006508biological_processproteolysis
A0007369biological_processgastrulation
A0009083biological_processbranched-chain amino acid catabolic process
A0016491molecular_functionoxidoreductase activity
A0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A0031410cellular_componentcytoplasmic vesicle
A0031514cellular_componentmotile cilium
A0042391biological_processregulation of membrane potential
A0042995cellular_componentcell projection
A0043159cellular_componentacrosomal matrix
A0045252cellular_componentoxoglutarate dehydrogenase complex
A0045254cellular_componentpyruvate dehydrogenase complex
A0047101molecular_functionobsolete branched-chain alpha-keto acid dehydrogenase activity
A0048240biological_processsperm capacitation
A0050660molecular_functionflavin adenine dinucleotide binding
A0120551biological_process2-oxoglutarate decarboxylation to succinyl-CoA
A0120552biological_processbranched-chain alpha-keto acid decarboxylation to branched-chain acyl-CoA
A0160157cellular_componentbranched-chain alpha-ketoacid dehydrogenase complex
A0160167cellular_componentoxoadipate dehydrogenase complex
A1902493cellular_componentacetyltransferase complex
B0001669cellular_componentacrosomal vesicle
B0004148molecular_functiondihydrolipoyl dehydrogenase (NADH) activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005929cellular_componentcilium
B0006086biological_processpyruvate decarboxylation to acetyl-CoA
B0006103biological_process2-oxoglutarate metabolic process
B0006120biological_processmitochondrial electron transport, NADH to ubiquinone
B0006508biological_processproteolysis
B0007369biological_processgastrulation
B0009083biological_processbranched-chain amino acid catabolic process
B0016491molecular_functionoxidoreductase activity
B0016668molecular_functionoxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B0031410cellular_componentcytoplasmic vesicle
B0031514cellular_componentmotile cilium
B0042391biological_processregulation of membrane potential
B0042995cellular_componentcell projection
B0043159cellular_componentacrosomal matrix
B0045252cellular_componentoxoglutarate dehydrogenase complex
B0045254cellular_componentpyruvate dehydrogenase complex
B0047101molecular_functionobsolete branched-chain alpha-keto acid dehydrogenase activity
B0048240biological_processsperm capacitation
B0050660molecular_functionflavin adenine dinucleotide binding
B0120551biological_process2-oxoglutarate decarboxylation to succinyl-CoA
B0120552biological_processbranched-chain alpha-keto acid decarboxylation to branched-chain acyl-CoA
B0160157cellular_componentbranched-chain alpha-ketoacid dehydrogenase complex
B0160167cellular_componentoxoadipate dehydrogenase complex
B1902493cellular_componentacetyltransferase complex
Functional Information from PROSITE/UniProt
site_idPS00076
Number of Residues11
DetailsPYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCLnvGCIP
ChainResidueDetails
AGLY42-PRO52
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P09624","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues54
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15946682","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsSite: {"description":"Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex","evidences":[{"source":"PubMed","id":"20385101","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues14
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"O08749","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues10
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"O08749","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O08749","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q6P6R2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O08749","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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