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2G1H

Structure of E.coli FabD complexed with glycerol

Functional Information from GO Data
ChainGOidnamespacecontents
A0004314molecular_function[acyl-carrier-protein] S-malonyltransferase activity
A0005829cellular_componentcytosol
A0006633biological_processfatty acid biosynthetic process
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 310
ChainResidue
AGLY10
AHOH311
AHOH469
AGLN11
AHIS91
ASER92
ALEU93
AARG117
AMET121
ASER200
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
DetailsAnnotated By Reference To The Literature 1mla
ChainResidueDetails
AHIS201
ASER92
AGLN250

site_idMCSA1
Number of Residues6
DetailsM-CSA 291
ChainResidueDetails
AGLY12electrostatic stabiliser, hydrogen bond donor
ALEU93activator, covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
AGLY94electrostatic stabiliser, hydrogen bond donor
AGLY118attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
ACYS202hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity, proton acceptor, proton donor
ALEU251electrostatic stabiliser, hydrogen bond acceptor, increase basicity

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PDB entries from 2024-07-03

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