5EY9
Structure of FadD32 from Mycobacterium marinum complexed to AMPC12
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0008610 | biological_process | lipid biosynthetic process |
| A | 0008922 | molecular_function | long-chain fatty acid [acyl-carrier-protein] ligase activity |
| A | 0016874 | molecular_function | ligase activity |
| A | 0070566 | molecular_function | adenylyltransferase activity |
| A | 0071766 | biological_process | Actinobacterium-type cell wall biogenesis |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0008610 | biological_process | lipid biosynthetic process |
| B | 0008922 | molecular_function | long-chain fatty acid [acyl-carrier-protein] ligase activity |
| B | 0016874 | molecular_function | ligase activity |
| B | 0070566 | molecular_function | adenylyltransferase activity |
| B | 0071766 | biological_process | Actinobacterium-type cell wall biogenesis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue 5SV A 701 |
| Chain | Residue |
| A | HIS230 |
| A | TYR342 |
| A | GLY343 |
| A | LEU344 |
| A | ALA345 |
| A | LEU349 |
| A | ASP468 |
| A | ILE479 |
| A | ARG482 |
| A | LYS600 |
| A | HOH869 |
| A | ASP231 |
| A | HOH915 |
| A | HOH976 |
| A | HOH984 |
| A | MET232 |
| A | SER278 |
| A | LEU310 |
| A | SER313 |
| A | GLU314 |
| A | PRO315 |
| A | SER341 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 702 |
| Chain | Residue |
| A | ASP397 |
| A | GLU398 |
| A | TRP399 |
| A | HOH871 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 703 |
| Chain | Residue |
| A | ASP413 |
| A | PHE473 |
| A | LYS474 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 704 |
| Chain | Residue |
| A | ARG268 |
| A | THR273 |
| A | GLY274 |
| A | SER304 |
| A | ASN305 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 705 |
| Chain | Residue |
| A | VAL156 |
| A | ILE157 |
| A | ALA158 |
| A | ALA161 |
| A | VAL162 |
| B | VAL378 |
| B | ALA382 |
| B | HOH832 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | binding site for residue 5SV B 701 |
| Chain | Residue |
| B | VAL210 |
| B | HIS230 |
| B | ASP231 |
| B | THR236 |
| B | SER278 |
| B | LEU310 |
| B | SER313 |
| B | GLU314 |
| B | PRO315 |
| B | SER341 |
| B | TYR342 |
| B | GLY343 |
| B | LEU344 |
| B | LEU349 |
| B | ASP468 |
| B | ILE479 |
| B | ARG482 |
| B | LYS600 |
| B | HOH846 |
| B | HOH882 |
| B | HOH977 |
| B | HOH982 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 702 |
| Chain | Residue |
| B | GLY395 |
| B | ASP397 |
| B | GLU398 |
| B | TRP399 |
| B | HOH889 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 703 |
| Chain | Residue |
| B | ASP413 |
| B | PHE473 |
| B | LYS474 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 704 |
| Chain | Residue |
| B | GLU139 |
| B | ARG268 |
| B | THR273 |
| B | GLY274 |
| B | ASN305 |
| B | ARG334 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"A0R618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
