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 | Active site: {"evidences":[{"source":"PubMed","id":"7768883","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 | GLN11 | electrostatic stabiliser, hydrogen bond donor |
| A | SER92 | activator, covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | LEU93 | electrostatic stabiliser, hydrogen bond donor |
| A | ARG117 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| A | HIS201 | hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity, proton acceptor, proton donor |
| A | GLN250 | electrostatic stabiliser, hydrogen bond acceptor, increase basicity |






