Research workbench
The crystal structure of human quinolinic acid phosphoribosyltransferase in complex with its inhibitor phthalic acid
Analyse The crystal structure of human quinolinic acid phosphoribosyltransferase in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KWW
- Type
- protein
- Length
- 1,708 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- EC
- 2.4.2.19
- UniProt
- Q15274
- Ligands
- PHT
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, F | Nicotinate-nucleotide pyrophosphorylase [carboxylating] (EC 2.4.2.19) | protein | 285 | 45% helix, 19% strand | Q15274 |
| D, E | Nicotinate-nucleotide pyrophosphorylase [carboxylating] (EC 2.4.2.19) | protein | 284 | 45% helix, 19% strand | Q15274 |
Ligands and binding sites
- PHT · Phthalic acid · ligand · 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
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 839 | 0.81 | 0.84 | 95 | empty |
| 2 | 125 | 0.78 | 0.97 | 44 | empty |
| 3 | 114 | 0.77 | 0.96 | 27 | empty |
| 4 | 97 | 0.74 | 0.96 | 24 | empty |
| 5 | 80 | 0.73 | 0.97 | 33 | empty |
Interfaces
15 interfaces between chains.
- E–F · 2534 Ų buried · 41 hydrogen bonds · protein-protein
- A–B · 2533 Ų buried · 42 hydrogen bonds · protein-protein
- C–D · 2518 Ų buried · 41 hydrogen bonds · protein-protein
- D–E · 659 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 659 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 4KWW · The crystal structure of human quinolinic acid phosphoribosyltransferase in complex with… · the same entry in another collection · chain F against F, TM-score 1.00
- Q15274 · AlphaFold monomer V2.0 prediction for nicotinate-nucleotide pyrophosphorylase… · 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 Q15274
- Elsewhere: RCSB PDB 4KWW · PDBe 4KWW · UniProt Q15274
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