6U0J
Crosslinked Crystal Structure of Malonyl-CoA Acyl Carrier Protein Transacylase, FabD, and Acyl Carrier Protein, AcpP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004314 | molecular_function | [acyl-carrier-protein] S-malonyltransferase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| B | 0000035 | molecular_function | acyl binding |
| B | 0000036 | molecular_function | acyl carrier activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0008289 | molecular_function | lipid binding |
| B | 0008610 | biological_process | lipid biosynthetic process |
| B | 0009245 | biological_process | lipid A biosynthetic process |
| B | 0009410 | biological_process | response to xenobiotic stimulus |
| B | 0016020 | cellular_component | membrane |
| B | 0031177 | molecular_function | phosphopantetheine binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 401 |
| Chain | Residue |
| A | MET18 |
| A | LEU19 |
| A | PRO277 |
| A | GLY278 |
| A | ASN298 |
| A | HOH518 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | ALA84 |
| A | PRO85 |
| A | ALA86 |
| A | HOH532 |
| A | HOH606 |
| A | HOH649 |
| A | GLN3 |
| A | PHE4 |
| A | LYS83 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | GLU31 |
| A | GLN79 |
| A | ASN239 |
| A | HOH643 |
| A | HOH652 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | GLN3 |
| A | GLN267 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | PRO224 |
| A | HOH505 |
| A | HOH629 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 406 |
| Chain | Residue |
| A | GLN11 |
| A | CYS92 |
| A | LEU93 |
| A | ARG117 |
| A | SER200 |
| A | HIS201 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | LYS83 |
| A | THR220 |
| A | HOH513 |
| A | HOH540 |
| A | HOH581 |
| A | HOH679 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 408 |
| Chain | Residue |
| A | HOH506 |
| A | HOH685 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | binding site for residue 9EF B 101 |
| Chain | Residue |
| A | GLN11 |
| A | HIS91 |
| A | CYS92 |
| A | ASN160 |
| A | ASN162 |
| A | GLN166 |
| A | VAL168 |
| A | LEU192 |
| A | HIS201 |
| A | HOH578 |
| A | HOH600 |
| B | ASP35 |
| B | SER36 |
| B | HOH220 |
| B | HOH223 |
Functional Information from PROSITE/UniProt
| site_id | PS00012 |
| Number of Residues | 16 |
| Details | PHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGADSLDTVELVMAL |
| Chain | Residue | Details |
| B | ASP31-LEU46 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | MOD_RES: O-(pantetheine 4'-phosphoryl)serine => ECO:0000255|PROSITE-ProRule:PRU00258, ECO:0000269|PubMed:4882207 |
| Chain | Residue | Details |
| B | SER36 | |
| A | HIS201 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 291 |
| Chain | Residue | Details |
| A | GLN11 | electrostatic stabiliser, hydrogen bond donor |
| A | CYS92 | 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 |
