Research workbench
Crystal structure of VISFATIN/PRE-B cell colony enhancing factor 1/NICOTINAMIDE phosphoribosyltransferase
Analyse Crystal structure of VISFATIN/PRE-B cell colony enhancing factor 1/NICOTINAMIDE… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G95
- Type
- protein
- Length
- 916 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nicotinamide phosphoribosyltransferase
- EC
- 2.4.2.12
- UniProt
- Q80Z29
- Pockets
- 9 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nicotinamide phosphoribosyltransferase (EC 2.4.2.12) | protein | 456 | 43% helix, 19% strand | Q80Z29 |
| B | Nicotinamide phosphoribosyltransferase (EC 2.4.2.12) | protein | 460 | 42% helix, 18% strand | Q80Z29 |
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 | 734 | 0.75 | 0.80 | 65 | empty |
| 2 | 845 | 0.73 | 0.78 | 68 | empty |
| 3 | 618 | 0.70 | 0.79 | 46 | empty |
| 4 | 335 | 0.65 | 0.80 | 39 | empty |
| 5 | 315 | 0.64 | 0.80 | 38 | empty |
Interfaces
1 interface between chains.
- A–B · 3491 Ų buried · 60 hydrogen bonds · protein-protein
Compared structures
- 2G95 · Crystal Structure of Visfatin/Pre-B Cell Colony Enhancing Factor 1/Nicotinamide… · the same entry in another collection · chain A against A, TM-score 1.00
- Q80Z29 · AlphaFold monomer V2.0 prediction for nicotinamide phosphoribosyltransferase (Q80Z29) · 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 Q80Z29
- Elsewhere: RCSB PDB 2G95 · PDBe 2G95 · UniProt Q80Z29
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