Research workbench
Quinolinate phosphoribosyl transferase (qaprtase) apo-enzyme from mycobacterium tuberculosis
Analyse Quinolinate phosphoribosyl transferase (qaprtase) apo-enzyme from mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QPO
- Type
- protein
- Length
- 1,704 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Quinolinate acid phosphoribosyl transferase
- EC
- 2.4.2.19
- UniProt
- O06594
- Ligands
- SO4
- Pockets
- 9 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Quinolinate acid phosphoribosyl transferase (EC 2.4.2.19) | protein | 284 | 45% helix, 20% strand | O06594 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1120 | 0.83 | 0.84 | 120 | SO4 |
| 2 | 461 | 0.80 | 0.87 | 48 | SO4 |
| 3 | 500 | 0.79 | 0.86 | 66 | SO4 |
| 4 | 570 | 0.79 | 0.85 | 70 | SO4 |
| 5 | 454 | 0.74 | 0.84 | 54 | SO4 |
Interfaces
12 interfaces between chains.
- C–D · 2576 Ų buried · 33 hydrogen bonds · protein-protein
- E–F · 2568 Ų buried · 36 hydrogen bonds · protein-protein
- A–B · 2540 Ų buried · 34 hydrogen bonds · protein-protein
- A–E · 268 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 267 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1QPO · Quinolinate Phosphoribosyl Transferase (QAPRTase) Apo-Enzyme from Mycobacterium… · 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 O06594
- Elsewhere: RCSB PDB 1QPO · PDBe 1QPO · UniProt O06594
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