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1MLA

THE ESCHERICHIA COLI MALONYL-COA:ACYL CARRIER PROTEIN TRANSACYLASE AT 1.5-ANGSTROMS RESOLUTION. CRYSTAL STRUCTURE OF A FATTY ACID SYNTHASE COMPONENT

Functional Information from GO Data
ChainGOidnamespacecontents
A0004314molecular_function[acyl-carrier-protein] S-malonyltransferase activity
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
Functional Information from PDB Data
site_idCAT
Number of Residues2
DetailsCATALYTIC DYAD
ChainResidue
ASER92
AHIS201

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:7768883
ChainResidueDetails
ALEU93
ACYS202

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 7768883
ChainResidueDetails
ASER92
AHIS201
AGLN250

site_idMCSA1
Number of Residues6
DetailsM-CSA 291
ChainResidueDetails
AGLN11electrostatic stabiliser, hydrogen bond donor
ASER92activator, covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
ALEU93electrostatic stabiliser, hydrogen bond donor
AARG117attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
AHIS201hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity, proton acceptor, proton donor
AGLN250electrostatic stabiliser, hydrogen bond acceptor, increase basicity

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PDB entries from 2025-06-18

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