2G1H
Structure of E.coli FabD complexed with glycerol
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GOL A 310 |
Chain | Residue |
A | GLY10 |
A | HOH311 |
A | HOH469 |
A | GLN11 |
A | HIS91 |
A | SER92 |
A | LEU93 |
A | ARG117 |
A | MET121 |
A | SER200 |
A | HIS201 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:7768883 |
Chain | Residue | Details |
A | LEU93 | |
A | CYS202 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1mla |
Chain | Residue | Details |
A | HIS201 | |
A | SER92 | |
A | GLN250 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 291 |
Chain | Residue | Details |
A | GLY12 | electrostatic stabiliser, hydrogen bond donor |
A | LEU93 | activator, covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
A | GLY94 | electrostatic stabiliser, hydrogen bond donor |
A | GLY118 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
A | CYS202 | hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity, proton acceptor, proton donor |
A | LEU251 | electrostatic stabiliser, hydrogen bond acceptor, increase basicity |