MolNFT v1 · #102804 · protein
Anthranilate phosphoribosyl transferase from mycobacterium tuberculosis in complex with anthranilate
4OWV · Anthranilate phosphoribosyltransferase: “Anthranilate phosphoribosyl transferase from mycobacterium tuberculosis in complex with anthranilate”. X-ray diffraction, 2 ligands (BE2, PO4), 4 pockets (best druggability 0.74). MolNFT v1…
- PDB
- 4OWV
- Type
- protein
- Length
- 688 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anthranilate phosphoribosyltransferase
- EC
- 2.4.2.18
- UniProt
- P66992
- Ligands
- BE2, PO4
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Anthranilate phosphoribosyltransferase (EC 2.4.2.18) | protein | 343 | 53% helix, 12% strand | P66992 |
| B | Anthranilate phosphoribosyltransferase (EC 2.4.2.18) | protein | 345 | 54% helix, 12% strand | P66992 |
Ligands and binding sites
- BE2 · 2-aminobenzoic acid · ligand · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · chains B
- GOL · Glycerol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 657 | 0.74 | 0.80 | 62 | BE2 |
| 2 | 551 | 0.68 | 0.78 | 44 | BE2 |
| 3 | 89 | 0.40 | 0.77 | 19 | empty |
| 4 | 61 | 0.37 | 0.79 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 882 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 4OWV · Anthranilate phosphoribosyl transferase from Mycobacterium tuberculosis in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P66992
- Elsewhere: RCSB PDB 4OWV · PDBe 4OWV · UniProt P66992
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