MolNFT v1 · #19134 · protein
Quinolinic acid phosphoribosyltransferase with bound quinolinic acid
1QAP: “Quinolinic acid phosphoribosyltransferase with bound quinolinic acid”. X-ray diffraction, 1 ligand (NTM), 6 pockets (best druggability 0.73). MolNFT v1 #19134 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1QAP
- Type
- protein
- Length
- 578 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Quinolinic acid phosphoribosyltransferase
- EC
- 2.4.2.19
- UniProt
- P30012
- Ligands
- NTM
- Pockets
- 6 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Quinolinic acid phosphoribosyltransferase (EC 2.4.2.19) | protein | 289 | 46% helix, 18% strand | P30012 |
Ligands and binding sites
- NTM · Quinolinic acid · ligand · 2 copies · chains A, 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 624 | 0.73 | 0.80 | 59 | NTM |
| 2 | 513 | 0.71 | 0.81 | 50 | NTM |
| 3 | 155 | 0.61 | 0.84 | 38 | empty |
| 4 | 123 | 0.44 | 0.77 | 22 | empty |
| 5 | 95 | 0.40 | 0.77 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 2577 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 1QAP · Quinolinic acid phosphoribosyltransferase with bound quinolinic acid · the same entry in another collection · chain A against A, TM-score 1.00
- P30012 · AlphaFold monomer V2.0 prediction for nicotinate-nucleotide pyrophosphorylase… · 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 P30012
- Elsewhere: RCSB PDB 1QAP · PDBe 1QAP · UniProt P30012
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