4XTZ
Mycobacterium tuberculosis biotin ligase complexed with bisubstrate inhibitor 69 that has a fluorine in place of the ribose 2'OH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004077 | molecular_function | biotin-[acetyl-CoA-carboxylase] ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008284 | biological_process | positive regulation of cell population proliferation |
| A | 0009374 | molecular_function | biotin binding |
| A | 0016874 | molecular_function | ligase activity |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0036211 | biological_process | protein modification process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0004077 | molecular_function | biotin-[acetyl-CoA-carboxylase] ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008284 | biological_process | positive regulation of cell population proliferation |
| B | 0009374 | molecular_function | biotin binding |
| B | 0016874 | molecular_function | ligase activity |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0036211 | biological_process | protein modification process |
| B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | binding site for residue 594 A 301 |
| Chain | Residue |
| A | SER38 |
| A | GLY73 |
| A | TRP74 |
| A | ALA75 |
| A | GLN81 |
| A | ILE83 |
| A | LYS138 |
| A | GLY141 |
| A | ILE142 |
| A | LEU143 |
| A | VAL155 |
| A | THR39 |
| A | GLY156 |
| A | ASN158 |
| A | VAL166 |
| A | ASP167 |
| A | ALA170 |
| A | HOH477 |
| A | HOH506 |
| A | ASN40 |
| A | GLN63 |
| A | GLY66 |
| A | ARG67 |
| A | GLY68 |
| A | ARG69 |
| A | ARG72 |
| site_id | AC2 |
| Number of Residues | 29 |
| Details | binding site for residue 594 B 301 |
| Chain | Residue |
| A | HOH425 |
| B | SER38 |
| B | THR39 |
| B | ASN40 |
| B | GLN63 |
| B | GLY66 |
| B | ARG67 |
| B | GLY68 |
| B | ARG69 |
| B | ARG72 |
| B | GLY73 |
| B | TRP74 |
| B | ALA75 |
| B | GLN81 |
| B | ILE83 |
| B | ASN130 |
| B | LYS138 |
| B | GLY141 |
| B | ILE142 |
| B | LEU143 |
| B | VAL155 |
| B | GLY156 |
| B | ASN158 |
| B | VAL166 |
| B | ASP167 |
| B | ALA170 |
| B | HOH421 |
| B | HOH469 |
| B | HOH477 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:24723382 |
| Chain | Residue | Details |
| A | SER38 | |
| A | GLN63 | |
| A | ARG67 | |
| A | LYS138 | |
| B | SER38 | |
| B | GLN63 | |
| B | ARG67 | |
| B | LYS138 |
