Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4JAD

STRUCTURAL DETERMINATION OF THE A50T:S279G:S280K:V281K:K282E:H283N VARIANT OF CITRATE SYNTHASE from E. COLI

Replaces:  3L96
Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006099biological_processtricarboxylic acid cycle
A0016740molecular_functiontransferase activity
A0034214biological_processprotein hexamerization
A0036440molecular_functioncitrate synthase activity
A0042802molecular_functionidentical protein binding
A0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
A0070404molecular_functionNADH binding
B0003824molecular_functioncatalytic activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006099biological_processtricarboxylic acid cycle
B0016740molecular_functiontransferase activity
B0034214biological_processprotein hexamerization
B0036440molecular_functioncitrate synthase activity
B0042802molecular_functionidentical protein binding
B0046912molecular_functionacyltransferase activity, acyl groups converted into alkyl on transfer
B0070404molecular_functionNADH binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 2001
ChainResidue
ATHR413
AGLY414
ATYR415
AHOH2298
BLYS1055

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 2002
ChainResidue
AARG387
AHOH2194
AHIS229
AASN232
AARG299
AARG314

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 2003
ChainResidue
AHIS110
ATYR145
AARG163
ALYS167

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1501
ChainResidue
BHIS1229
BHIS1305
BARG1314
BARG1387

Functional Information from PROSITE/UniProt
site_idPS00480
Number of Residues13
DetailsCITRATE_SYNTHASE Citrate synthase signature. GFGHrVy.KnyDPR
ChainResidueDetails
AGLY302-ARG314

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10117","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

PDB statisticsPDBj update infoContact PDBjnumon