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
Functional Information from PDB Data
site_id | CAT |
Number of Residues | 2 |
Details | CATALYTIC DYAD |
Chain | Residue |
A | SER92 |
A | HIS201 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | LEU93 | |
A | CYS202 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | a catalytic site defined by CSA, PubMed 7768883 |
Chain | Residue | Details |
A | SER92 | |
A | HIS201 | |
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 |