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4JAE

STRUCTURAL DETERMINATION OF THE A50T:S279G:S280K:V281K:K282E:H283N VARIANT OF CITRATE SYNTHASE FROM E. COLI complexed WITH S-CARBOXYMETHYL-COA

Replaces:  3L97
Functional Information from GO Data
ChainGOidnamespacecontents
A0004108molecular_functioncitrate (Si)-synthase 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
B0004108molecular_functioncitrate (Si)-synthase 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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AHIS229
AASN232
AARG299
AHIS305
AARG314
AARG387

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
BTYR1415
ALYS55
BTHR1413
BGLY1414

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE CMC A 503
ChainResidue
ATHR106
ATHR108
AARG109
AHIS110
ATHR111
AMET112
AGLU158
AILE159
APHE162
AARG163
ALYS167
AGLN182
AASN189
ACYS206
AHOH666

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 2001
ChainResidue
AGLY414
BLYS1055
BHOH2118

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 2002
ChainResidue
BHIS1229
BASN1232
BHIS1305
BARG1387

site_idAC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE CMC B 2003
ChainResidue
BTHR1105
BTHR1106
BTHR1108
BARG1109
BHIS1110
BTHR1111
BMET1112
BTYR1145
BILE1159
BPHE1162
BARG1163
BLYS1167
BASN1189
BCYS1206
BHOH2133

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
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10117
ChainResidueDetails
AHIS305
AASP362
BHIS1305
BASP1362

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
AGLU282
BGLU1282

224004

PDB entries from 2024-08-21

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