Research workbench
Anthranilate phosphoribosyltransferase variant R193A from mycobacterium tuberculosis remains ligand-free when co-crystallised with prpp and mg
Analyse Anthranilate phosphoribosyltransferase variant R193A from mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4X5A
- Type
- protein
- Length
- 694 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anthranilate phosphoribosyltransferase
- EC
- 2.4.2.18
- UniProt
- A5U4M0
- Pockets
- 3 · best druggability 0.62
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 | 345 | 54% helix, 12% strand | A5U4M0 |
| B | Anthranilate phosphoribosyltransferase (EC 2.4.2.18) | protein | 349 | 53% helix, 12% strand | A5U4M0 |
Ligands and binding sites
- GOL · Glycerol · additive · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 369 | 0.62 | 0.78 | 49 | empty |
| 2 | 140 | 0.50 | 0.80 | 35 | empty |
| 3 | 68 | 0.30 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 860 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 4X5A · Anthranilate phosphoribosyltransferase variant R193A from Mycobacterium tuberculosis… · the same entry in another collection · chain A against A, TM-score 1.00
- A5U4M0 · AlphaFold monomer V2.0 prediction for anthranilate phosphoribosyltransferase (A5U4M0) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 A5U4M0
- Elsewhere: RCSB PDB 4X5A · PDBe 4X5A · UniProt A5U4M0
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