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3G0Y

Structure of E. coli FabF(C163Q) in complex with dihydroplatensimycin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004315molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006633biological_processfatty acid biosynthetic process
A0009409biological_processresponse to cold
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0019367biological_processfatty acid elongation, saturated fatty acid
A0042803molecular_functionprotein homodimerization activity
A0044281biological_processsmall molecule metabolic process
A1903966biological_processmonounsaturated fatty acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE P9A A 413
ChainResidue
AGLN163
AALA309
AGLY310
AHIS340
APHE398
AGLY399
APHE400
AHOH517
AHOH550
AHOH583
AALA205
AARG206
ATHR270
ASER271
APRO272
AHIS303
ATHR307
APRO308

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348, ECO:0000269|PubMed:10037680, ECO:0000305|PubMed:9482715
ChainResidueDetails
AGLN163

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348
ChainResidueDetails
AHIS303
AHIS340

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16710421, ECO:0000269|PubMed:19233644, ECO:0000269|PubMed:19581087, ECO:0007744|PDB:2GFX, ECO:0007744|PDB:3G0Y, ECO:0007744|PDB:3G11, ECO:0007744|PDB:3HNZ, ECO:0007744|PDB:3I8P
ChainResidueDetails
ATHR270
ATHR307

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16710421, ECO:0000269|PubMed:19233644, ECO:0007744|PDB:2GFX, ECO:0007744|PDB:3G0Y, ECO:0007744|PDB:3G11
ChainResidueDetails
AHIS303
AHIS340

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 574
ChainResidueDetails
AGLN163covalently 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 2024-05-15

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