Research workbench
Crystal structure of the quinolinate phosphoribosyl transferase (BNA6) from saccharomyces cerevisiae complexed with prpp
Analyse Crystal structure of the quinolinate phosphoribosyl transferase (BNA6) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C2F
- Type
- protein
- Length
- 267 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nicotinate-nucleotide pyrophosphorylase
- EC
- 2.4.2.19
- UniProt
- P43619
- Ligands
- PRP
- Pockets
- 5 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nicotinate-nucleotide pyrophosphorylase (EC 2.4.2.19) | protein | 267 | 41% helix, 20% strand | P43619 |
Ligands and binding sites
- PRP · 1-O-pyrophosphono-5-O-phosphono-alpha-D-ribofuranose · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 112 | 0.58 | 0.85 | 17 | empty |
| 2 | 130 | 0.43 | 0.77 | 21 | PRP |
| 3 | 65 | 0.34 | 0.76 | 11 | empty |
| 4 | 57 | 0.30 | 0.75 | 14 | empty |
| 5 | 54 | 0.26 | 0.72 | 21 | empty |
Compared structures
- 3C2F · Crystal structure of the quinolinate phosphoribosyl transferase (BNA6) from Saccharomyces… · the same entry in another collection · chain A against A, TM-score 1.00
- P43619 · AlphaFold monomer V2.0 prediction for nicotinate-nucleotide pyrophosphorylase… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P43619
- Elsewhere: RCSB PDB 3C2F · PDBe 3C2F · UniProt P43619
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