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6VEF

Cryo-EM Structure of Escherichia coli 2-oxoglutarate dehydrogenase E1 component sucA

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004591molecular_functionoxoglutarate dehydrogenase (succinyl-transferring) activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006099biological_processtricarboxylic acid cycle
A0016491molecular_functionoxidoreductase activity
A0016624molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
A0030976molecular_functionthiamine pyrophosphate binding
A0042802molecular_functionidentical protein binding
A0045252cellular_componentoxoglutarate dehydrogenase complex
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004591molecular_functionoxoglutarate dehydrogenase (succinyl-transferring) activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006099biological_processtricarboxylic acid cycle
B0016491molecular_functionoxidoreductase activity
B0016624molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
B0030976molecular_functionthiamine pyrophosphate binding
B0042802molecular_functionidentical protein binding
B0045252cellular_componentoxoglutarate dehydrogenase complex
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue AMP A 1001
ChainResidue
AHIS313
AARG337
ASER530
APHE531
ATRP533
ALEU537
ATHR673
AARG710
AMET711

site_idAC2
Number of Residues9
Detailsbinding site for residue OAA A 1002
ChainResidue
AGLU616
ALEU659
AGLN685
APHE689
BHIS260
BARG261
BASP357
BGLY393
BPHE394

site_idAC3
Number of Residues9
Detailsbinding site for residue OAA B 1001
ChainResidue
AHIS260
AARG261
AASP357
AGLY393
APHE394
BGLU616
BLEU659
BGLN685
BPHE689

site_idAC4
Number of Residues9
Detailsbinding site for residue AMP B 1002
ChainResidue
BHIS313
BARG337
BSER530
BPHE531
BTRP533
BLEU537
BTHR673
BARG710
BMET711

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: O-AMP-threonine; by ydiU => ECO:0000269|PubMed:30270044
ChainResidueDetails
APRO406
BPRO406

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PDB entries from 2024-10-16

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