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1KAS

BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0004315molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0009409biological_processresponse to cold
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0019367biological_processfatty acid elongation, saturated fatty acid
A0042803molecular_functionprotein homodimerization activity
A1903966biological_processmonounsaturated fatty acid biosynthetic process
Functional Information from PDB Data
site_idACT
Number of Residues1
DetailsACTIVE SITE RESIDUE.
ChainResidue
ACYS163

Functional Information from PROSITE/UniProt
site_idPS00606
Number of Residues17
DetailsKS3_1 Ketosynthase family 3 (KS3) active site signature. GPSisIAtACTSGvhNI
ChainResidueDetails
AGLY154-ILE170

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues409
DetailsDomain: {"description":"Ketosynthase family 3 (KS3)","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"For beta-ketoacyl synthase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10037680","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9482715","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"For beta-ketoacyl synthase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16710421","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19233644","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19581087","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2GFX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G0Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G11","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HNZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3I8P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16710421","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19233644","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2GFX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G0Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G11","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues7
Detailsa catalytic site defined by CSA, PubMed 15952903
ChainResidueDetails
ACYS163
ACYS163
APHE400
AHIS303
ALYS335
AGLU314
AHIS340

site_idMCSA1
Number of Residues6
DetailsM-CSA 574
ChainResidueDetails
ACYS163covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
AHIS303activator, proton acceptor, proton donor
AGLU314electrostatic stabiliser
ALYS335electrostatic stabiliser
AHIS340electrostatic stabiliser, hydrogen bond donor
APHE400electrostatic stabiliser

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PDB entries from 2025-07-16

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