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4YBO

Structure of Citrate Synthase from the Thermoacidophilic Euryarchaeon Thermolasma acidophilum

Functional Information from GO Data
ChainGOidnamespacecontents
A0004108molecular_functioncitrate (Si)-synthase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006099biological_processtricarboxylic acid cycle
A0016740molecular_functiontransferase activity
A0036440molecular_functioncitrate synthase activity
A0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
B0004108molecular_functioncitrate (Si)-synthase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006099biological_processtricarboxylic acid cycle
B0016740molecular_functiontransferase activity
B0036440molecular_functioncitrate synthase activity
B0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
C0004108molecular_functioncitrate (Si)-synthase activity
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005975biological_processcarbohydrate metabolic process
C0006099biological_processtricarboxylic acid cycle
C0016740molecular_functiontransferase activity
C0036440molecular_functioncitrate synthase activity
C0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
D0004108molecular_functioncitrate (Si)-synthase activity
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005975biological_processcarbohydrate metabolic process
D0006099biological_processtricarboxylic acid cycle
D0016740molecular_functiontransferase activity
D0036440molecular_functioncitrate synthase activity
D0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue BCT B 400
ChainResidue
BLYS286
BPRO287
BGLU288
BVAL289

site_idAC2
Number of Residues3
Detailsbinding site for residue BCT C 400
ChainResidue
CLYS286
CPRO287
CGLU288

Functional Information from PROSITE/UniProt
site_idPS00480
Number of Residues13
DetailsCITRATE_SYNTHASE Citrate synthase signature. GFGHrVy.KtyDPR
ChainResidueDetails
AGLY259-ARG271

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:7704526
ChainResidueDetails
AHIS222
DHIS222
DHIS262
DASP317
AHIS262
AASP317
BHIS222
BHIS262
BASP317
CHIS222
CHIS262
CASP317

224201

PDB entries from 2024-08-28

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