Research workbench
Anthranilate phosphoribosyltransferase variant R193L from mycobacterium tuberculosis in complex with prpp and mg
Analyse Anthranilate phosphoribosyltransferase variant R193L from mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4X5B
- Type
- protein
- Length
- 692 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
- Ligands
- PRP, MG
- Pockets
- 6 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Anthranilate phosphoribosyltransferase (EC 2.4.2.18) | protein | 346 | 53% helix, 12% strand | A5U4M0 |
Ligands and binding sites
- PRP · 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 484 | 0.76 | 0.85 | 49 | PRP, MG |
| 2 | 534 | 0.76 | 0.83 | 51 | PRP |
| 3 | 60 | 0.44 | 0.83 | 17 | empty |
| 4 | 65 | 0.41 | 0.81 | 17 | empty |
| 5 | 74 | 0.38 | 0.78 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 883 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 4X5B · Anthranilate phosphoribosyltransferase variant R193L from Mycobacterium tuberculosis in… · 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 0.99
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 4X5B · PDBe 4X5B · UniProt A5U4M0
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