4XU1
Mycobacterium tuberculosis biotin ligase complexed with bisubstrate inhibitor 82 that incorporates a morpholine in place of the ribose
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 | 25 |
Details | binding site for residue 44O A 301 |
Chain | Residue |
A | SER38 |
A | GLY73 |
A | TRP74 |
A | ALA75 |
A | GLN81 |
A | ILE83 |
A | LYS138 |
A | GLY141 |
A | ILE142 |
A | VAL155 |
A | GLY156 |
A | THR39 |
A | ASN158 |
A | VAL166 |
A | ASP167 |
A | ALA170 |
A | HOH519 |
A | HOH565 |
A | ASN40 |
A | GLN63 |
A | GLY66 |
A | ARG67 |
A | GLY68 |
A | ARG69 |
A | ARG72 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
A | PRO120 |
A | PRO121 |
A | ALA122 |
A | GLU123 |
A | THR124 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue DMS A 303 |
Chain | Residue |
A | HIS70 |
A | ARG72 |
A | GLU226 |
A | PRO228 |
A | ASP261 |
site_id | AC4 |
Number of Residues | 25 |
Details | binding site for residue 44O B 301 |
Chain | Residue |
B | SER38 |
B | THR39 |
B | ASN40 |
B | GLN63 |
B | GLY66 |
B | ARG67 |
B | GLY68 |
B | ARG69 |
B | ARG72 |
B | TRP74 |
B | ALA75 |
B | GLN81 |
B | ILE83 |
B | ASN130 |
B | LYS138 |
B | GLY141 |
B | ILE142 |
B | VAL155 |
B | GLY156 |
B | ASN158 |
B | VAL166 |
B | ASP167 |
B | ALA170 |
B | HOH540 |
B | HOH715 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue DMS B 302 |
Chain | Residue |
A | GLU193 |
B | GLY220 |
B | ARG222 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000305|PubMed:24723382 |
Chain | Residue | Details |
B | ARG67 | |
B | LYS138 | |
A | SER38 | |
A | GLN63 | |
A | ARG67 | |
A | LYS138 | |
B | SER38 | |
B | GLN63 |