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7WGR

Cryo-electron microscopic structure of the 2-oxoglutarate dehydrogenase (E1) component of the human alpha-ketoglutarate (2-oxoglutarate) dehydrogenase complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0016624molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
A0030976molecular_functionthiamine pyrophosphate binding
B0016624molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
B0030976molecular_functionthiamine pyrophosphate binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000305|PubMed:24495017
ChainResidueDetails
AASP154
BGLU179
BASP181
BASP183
AASP156
AASP158
AGLU179
AASP181
AASP183
BASP154
BASP156
BASP158

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q60597
ChainResidueDetails
ALYS401
BLYS401

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q60597
ChainResidueDetails
ALYS564
BLYS564

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS970
BLYS970

site_idSWS_FT_FI5
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:17370265
ChainResidueDetails
ALYS534
BLYS534

221716

PDB entries from 2024-06-26

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