MolNFT v1 · #28938 · protein
Crystal structure of a nicotinate phosphoribosyltransferase from thermoplasma acidophilum, phosphoribosylpyrophosphate bound structure
1YTE: “Crystal structure of a nicotinate phosphoribosyltransferase from thermoplasma acidophilum…”. X-ray diffraction, 1 ligand (PCP), 3 pockets (best druggability 0.50). MolNFT v1 #28938 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1YTE
- Type
- protein
- Length
- 389 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nicotinate phosphoribosyltransferase from thermoplasma acidophilum
- EC
- 2.4.2.11
- UniProt
- Q9HJ28
- Ligands
- PCP
- Pockets
- 3 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nicotinate phosphoribosyltransferase from thermoplasma acidophilum (EC 2.4.2.11) | protein | 389 | 39% helix, 21% strand | Q9HJ28 |
Ligands and binding sites
- PCP · 1-alpha-pyrophosphoryl-2-alpha,3-alpha-dihydroxy-4-beta-cyclopentane-methanol-5-phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 248 | 0.50 | 0.75 | 34 | empty |
| 2 | 134 | 0.45 | 0.77 | 23 | empty |
| 3 | 140 | 0.39 | 0.74 | 25 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1YTE · Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HJ28 · AlphaFold monomer V2.0 prediction for putative nicotinate phosphoribosyltransferase… · 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 Q9HJ28
- Elsewhere: RCSB PDB 1YTE · PDBe 1YTE · UniProt Q9HJ28
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