5HM3
2.25 Angstrom Resolution Crystal Structure of Long-chain-fatty-acid-AMP Ligase FadD32 from Mycobacterium tuberculosis in complex with Inhibitor 5'-O-[(11-phenoxyundecanoyl)sulfamoyl]adenosine
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 | 0009274 | cellular_component | peptidoglycan-based cell wall |
| A | 0016874 | molecular_function | ligase activity |
| A | 0070566 | molecular_function | adenylyltransferase activity |
| A | 0071766 | biological_process | Actinobacterium-type cell wall biogenesis |
| A | 0071769 | biological_process | mycolate cell wall layer assembly |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue 649 A 701 |
| Chain | Residue |
| A | LEU222 |
| A | TYR350 |
| A | GLY351 |
| A | LEU352 |
| A | ALA353 |
| A | LEU357 |
| A | ASP476 |
| A | LYS608 |
| A | HOH857 |
| A | HOH867 |
| A | HOH882 |
| A | HIS238 |
| A | ASP239 |
| A | LEU247 |
| A | ALA248 |
| A | SER321 |
| A | GLU322 |
| A | PRO323 |
| A | SER349 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 702 |
| Chain | Residue |
| A | ARG55 |
| A | THR281 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 703 |
| Chain | Residue |
| A | ARG500 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 A 704 |
| Chain | Residue |
| A | ARG70 |
| A | ASP97 |
| A | ILE100 |
| A | ASP168 |
| A | HIS567 |
| A | HOH807 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 A 705 |
| Chain | Residue |
| A | ARG265 |
| A | ARG266 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 A 706 |
| Chain | Residue |
| A | SER195 |
| A | ARG490 |
| A | LYS492 |
| A | HOH804 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue PEG A 707 |
| Chain | Residue |
| A | HIS123 |
| A | ARG126 |
| A | SER195 |
| A | THR604 |
| A | SER605 |
| A | SER606 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 708 |
| Chain | Residue |
| A | GLU294 |
| A | ARG519 |
| A | VAL520 |
| A | HOH850 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 709 |
| Chain | Residue |
| A | LEU44 |
| A | HIS253 |
| A | SER254 |
| A | SER636 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"A0R618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"27590338","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
