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6PBR

Catalytic domain of E.coli dihydrolipoamide succinyltransferase in I4 space group

Functional Information from GO Data
ChainGOidnamespacecontents
A0004149molecular_functiondihydrolipoyllysine-residue succinyltransferase activity
A0006099biological_processtricarboxylic acid cycle
A0016746molecular_functionacyltransferase activity
A0045252cellular_componentoxoglutarate dehydrogenase complex
B0004149molecular_functiondihydrolipoyllysine-residue succinyltransferase activity
B0006099biological_processtricarboxylic acid cycle
B0016746molecular_functionacyltransferase activity
B0045252cellular_componentoxoglutarate dehydrogenase complex
C0004149molecular_functiondihydrolipoyllysine-residue succinyltransferase activity
C0006099biological_processtricarboxylic acid cycle
C0016746molecular_functionacyltransferase activity
C0045252cellular_componentoxoglutarate dehydrogenase complex
D0004149molecular_functiondihydrolipoyllysine-residue succinyltransferase activity
D0006099biological_processtricarboxylic acid cycle
D0016746molecular_functionacyltransferase activity
D0045252cellular_componentoxoglutarate dehydrogenase complex
E0004149molecular_functiondihydrolipoyllysine-residue succinyltransferase activity
E0006099biological_processtricarboxylic acid cycle
E0016746molecular_functionacyltransferase activity
E0045252cellular_componentoxoglutarate dehydrogenase complex
F0004149molecular_functiondihydrolipoyllysine-residue succinyltransferase activity
F0006099biological_processtricarboxylic acid cycle
F0016746molecular_functionacyltransferase activity
F0045252cellular_componentoxoglutarate dehydrogenase complex
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue NA A 501
ChainResidue
ALYS391
AGLU395
BLYS351

site_idAC2
Number of Residues1
Detailsbinding site for residue NA B 501
ChainResidue
BGLU395

site_idAC3
Number of Residues1
Detailsbinding site for residue NA D 501
ChainResidue
DGLU395

site_idAC4
Number of Residues2
Detailsbinding site for residue NA E 501
ChainResidue
EGLU395
FLYS351

site_idAC5
Number of Residues2
Detailsbinding site for residue NA F 501
ChainResidue
FLYS391
FGLU395

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:10739245, ECO:0000305|PubMed:9677295
ChainResidueDetails
AHIS375
AASP379
BHIS375
BASP379
CHIS375
CASP379
DHIS375
DASP379
EHIS375
EASP379
FHIS375
FASP379

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 704
ChainResidueDetails
ATHR323electrostatic stabiliser, polar interaction
AHIS375activator, proton acceptor, proton donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 704
ChainResidueDetails
BTHR323electrostatic stabiliser, polar interaction
BHIS375activator, proton acceptor, proton donor

site_idMCSA3
Number of Residues2
DetailsM-CSA 704
ChainResidueDetails
CTHR323electrostatic stabiliser, polar interaction
CHIS375activator, proton acceptor, proton donor

site_idMCSA4
Number of Residues2
DetailsM-CSA 704
ChainResidueDetails
DTHR323electrostatic stabiliser, polar interaction
DHIS375activator, proton acceptor, proton donor

site_idMCSA5
Number of Residues2
DetailsM-CSA 704
ChainResidueDetails
ETHR323electrostatic stabiliser, polar interaction
EHIS375activator, proton acceptor, proton donor

site_idMCSA6
Number of Residues2
DetailsM-CSA 704
ChainResidueDetails
FTHR323electrostatic stabiliser, polar interaction
FHIS375activator, proton acceptor, proton donor

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PDB entries from 2024-05-01

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