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 | 0005829 | cellular_component | cytosol |
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 | 5 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:A0R618 |
Chain | Residue | Details |
A | THR194 | |
A | SER349 | |
A | ALA353 | |
A | ASP476 | |
A | ARG490 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:27590338 |
Chain | Residue | Details |
A | THR552 |