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4G6B

Three dimensional structure analysis of the type II citrate synthase from e.coli

Replaces:  1K3P
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 Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AASN232
AALA233
AARG299
AARG306
AHOH604
AHOH788
AHOH800
BARG407

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 502
ChainResidue
ATYR145
AARG163
ALYS167
AHOH762
AHIS110

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 503
ChainResidue
AHIS229
AASN232
ALEU259
AARG299
AHIS305
AARG314
AARG387
AHOH788
AHOH795
AHOH924

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 2001
ChainResidue
AARG407
BASN232
BALA233
BARG299
BARG306

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 2002
ChainResidue
BHIS110
BTYR145
BARG163
BLYS167
BHOH2103
BHOH2495

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 2003
ChainResidue
BHIS229
BASN232
BARG299
BHIS305
BARG314
BARG387
BHOH2252
BHOH2299

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
BHIS305
BASP362

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS282
BLYS282

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PDB entries from 2024-09-11

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