5ICR
2.25 Angstrom Resolution Crystal Structure of Fatty-Acid-CoA Ligase (FadD32) from Mycobacterium smegmatis in complex with Inhibitor 5'-O-[(11-phenoxyundecanoyl)sulfamoyl]adenosine.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic 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 |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic 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 |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0006631 | biological_process | fatty acid metabolic process |
| C | 0008610 | biological_process | lipid biosynthetic process |
| C | 0008922 | molecular_function | long-chain fatty acid [acyl-carrier-protein] ligase activity |
| C | 0016874 | molecular_function | ligase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0006631 | biological_process | fatty acid metabolic process |
| D | 0008610 | biological_process | lipid biosynthetic process |
| D | 0008922 | molecular_function | long-chain fatty acid [acyl-carrier-protein] ligase activity |
| D | 0016874 | molecular_function | ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue 649 A 701 |
| Chain | Residue |
| A | LEU215 |
| A | GLU315 |
| A | PRO316 |
| A | ILE317 |
| A | SER342 |
| A | TYR343 |
| A | GLY344 |
| A | LEU345 |
| A | ALA346 |
| A | LEU350 |
| A | ASP469 |
| A | GLY223 |
| A | ILE480 |
| A | ARG483 |
| A | LYS601 |
| A | HOH955 |
| A | HOH1044 |
| A | HOH1075 |
| A | HIS231 |
| A | ASP232 |
| A | THR237 |
| A | LEU240 |
| A | ILE278 |
| A | LEU311 |
| A | SER314 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 702 |
| Chain | Residue |
| A | ASN372 |
| A | GLY374 |
| A | TYR470 |
| A | HOH826 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 703 |
| Chain | Residue |
| A | GLY396 |
| A | GLU399 |
| A | TRP400 |
| A | HOH967 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | binding site for residue 649 B 701 |
| Chain | Residue |
| B | THR187 |
| B | LEU215 |
| B | HIS231 |
| B | ASP232 |
| B | THR237 |
| B | LEU240 |
| B | ALA241 |
| B | SER314 |
| B | GLU315 |
| B | PRO316 |
| B | SER342 |
| B | TYR343 |
| B | GLY344 |
| B | LEU345 |
| B | ALA346 |
| B | LEU350 |
| B | ASP469 |
| B | ARG483 |
| B | LYS601 |
| B | HOH878 |
| B | HOH935 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 703 |
| Chain | Residue |
| B | VAL417 |
| B | TYR470 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | binding site for residue 649 C 701 |
| Chain | Residue |
| C | LEU215 |
| C | GLY223 |
| C | HIS231 |
| C | ASP232 |
| C | THR237 |
| C | LEU240 |
| C | ILE278 |
| C | LEU311 |
| C | SER314 |
| C | GLU315 |
| C | PRO316 |
| C | ILE317 |
| C | SER342 |
| C | TYR343 |
| C | GLY344 |
| C | LEU345 |
| C | ALA346 |
| C | LEU350 |
| C | ASP469 |
| C | ILE480 |
| C | ARG483 |
| C | LYS601 |
| C | HOH817 |
| C | HOH863 |
| C | HOH866 |
| C | HOH958 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 C 702 |
| Chain | Residue |
| C | VAL417 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue GOL C 703 |
| Chain | Residue |
| C | SER19 |
| C | SER20 |
| C | ILE21 |
| C | ALA205 |
| site_id | AC9 |
| Number of Residues | 22 |
| Details | binding site for residue 649 D 701 |
| Chain | Residue |
| D | ALA346 |
| D | LEU350 |
| D | ASP469 |
| D | ILE480 |
| D | ARG483 |
| D | LYS601 |
| D | HOH883 |
| D | HOH918 |
| D | HOH925 |
| D | HOH968 |
| D | LEU215 |
| D | HIS231 |
| D | ASP232 |
| D | THR237 |
| D | LEU240 |
| D | SER314 |
| D | GLU315 |
| D | PRO316 |
| D | ILE317 |
| D | SER342 |
| D | GLY344 |
| D | LEU345 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 D 702 |
| Chain | Residue |
| D | ASN372 |
| D | ASN494 |
| D | HOH852 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26628098, ECO:0007744|PDB:5D6J |
| Chain | Residue | Details |
| A | THR187 | |
| B | ARG483 | |
| C | THR187 | |
| C | SER342 | |
| C | ALA346 | |
| C | ASP469 | |
| C | ARG483 | |
| D | THR187 | |
| D | SER342 | |
| D | ALA346 | |
| D | ASP469 | |
| A | SER342 | |
| D | ARG483 | |
| A | ALA346 | |
| A | ASP469 | |
| A | ARG483 | |
| B | THR187 | |
| B | SER342 | |
| B | ALA346 | |
| B | ASP469 |
