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1C4T

CATALYTIC DOMAIN FROM TRIMERIC DIHYDROLIPOAMIDE SUCCINYLTRANSFERASE

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1101
ChainResidue
AHIS375
AGLY380
AHOH1019
AHOH1021

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1102
ChainResidue
ALEU278
BHIS375
BGLY380
BHOH1017
BHOH1028

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 1103
ChainResidue
BLEU278
CHIS375
CHOH1024

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1104
ChainResidue
AGLU250
ALEU377
AASP379
AGLU382

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1105
ChainResidue
BGLU250
BLEU377
BASP379
BGLU382

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 1106
ChainResidue
CGLU250
CLEU377
CASP379

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:10739245, ECO:0000305|PubMed:9677295
ChainResidueDetails
AHIS375
AASP379
BHIS375
BASP379
CHIS375
CASP379

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 10739245
ChainResidueDetails
AHIS375
CTHR323

site_idCSA2
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 10739245
ChainResidueDetails
BHIS375

site_idCSA3
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 10739245
ChainResidueDetails
CHIS375

site_idCSA4
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 10739245
ChainResidueDetails
AHIS375
CTHR323

site_idCSA5
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 10739245
ChainResidueDetails
ATHR323

site_idCSA6
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 10739245
ChainResidueDetails
BTHR323

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

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PDB entries from 2025-06-11

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