Research workbench
Anthranilate phosphoribosyltransferase (trpd) from mycobacterium tuberculosis (apo structure)
Analyse Anthranilate phosphoribosyltransferase (trpd) from mycobacterium tuberculosis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BPQ
- Type
- protein
- Length
- 683 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
- BEN
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Anthranilate phosphoribosyltransferase (EC 2.4.2.18) | protein | 344 | 52% helix, 13% strand | P66992 |
| B | Anthranilate phosphoribosyltransferase (EC 2.4.2.18) | protein | 339 | 52% helix, 12% strand | P66992 |
Ligands and binding sites
- BEN · Benzamidine · ligand · 3 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A, 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 527 | 0.79 | 0.86 | 56 | empty |
| 2 | 568 | 0.71 | 0.80 | 67 | BEN |
| 3 | 123 | 0.53 | 0.81 | 22 | BEN, GOL |
| 4 | 53 | 0.39 | 0.82 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 979 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2BPQ · Anthranilate phosphoribosyltransferase (TrpD) from Mycobacterium tuberculosis (Apo… · 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 2BPQ · PDBe 2BPQ · UniProt P66992
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