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1X7Y

Crystal structure of the human mitochondrial branched-chain alpha-ketoacid dehydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003863molecular_functionbranched-chain 2-oxo acid dehydrogenase activity
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0009083biological_processbranched-chain amino acid catabolic process
A0016491molecular_functionoxidoreductase activity
A0016624molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
A0016831molecular_functioncarboxy-lyase activity
A0046872molecular_functionmetal ion binding
A0047101molecular_functionobsolete branched-chain alpha-keto acid dehydrogenase activity
A0120552biological_processbranched-chain alpha-keto acid decarboxylation to branched-chain acyl-CoA
A0160157cellular_componentbranched-chain alpha-ketoacid dehydrogenase complex
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 801
ChainResidue
AGLN112
ASER161
APRO163
ATHR166
AGLN167
AHOH906

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K B 802
ChainResidue
BCYS178
BASP181
BASN183
BHOH1024
BGLY128
BLEU130
BTHR131

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 803
ChainResidue
AGLU193
AASN222
ATYR224
ATPP901
AHOH915

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 804
ChainResidue
ATYR113
ATPP901
BTYR102
BHIS146

site_idAC5
Number of Residues26
DetailsBINDING SITE FOR RESIDUE TPP A 901
ChainResidue
AARG114
ASER162
ALEU164
AGLY192
AGLU193
AGLY194
AALA195
AGLU198
AARG220
AASN222
ATYR224
AALA225
AILE226
AMN803
ACL804
AHOH915
AHOH931
AHOH957
AHOH965
AHOH977
AHOH1032
BGLU46
BLEU74
BGLU76
BGLN98
BTYR102

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 1001
ChainResidue
AGLN374
BTRP260
BTHR284
BGLU290
BTHR294
BARG309
BHOH1059

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10745006","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DTW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P50136","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q6P3A8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
BGLU76

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1dtw
ChainResidueDetails
BGLU76
BHIS146

site_idMCSA1
Number of Residues2
DetailsM-CSA 280
ChainResidueDetails
AGLU76activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, steric role
ASER162hydrogen bond acceptor, steric role

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PDB entries from 2025-07-09

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