MolNFT v1 · #22548 · protein
1.8 a crystal structure of an uncharacterized B. stearothermophilus protein
1T8H · Ylmd protein sequence homologue: “1.8 a crystal structure of an uncharacterized B. stearothermophilus protein”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.48). MolNFT v1 #22548 on GenesisL1: 3D structure…
- PDB
- 1T8H
- Type
- protein
- Length
- 272 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ylmd protein sequence homologue
- UniProt
- P84138
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ylmd protein sequence homologue | protein | 272 | 27% helix, 25% strand | P84138 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 146 | 0.48 | 0.78 | 18 | BME |
Modifications
Observed in the structure: 2 covalent (additive adduct).
Compared structures
- 1T8H · 1.8 a crystal structure of an uncharacterized B. stearothermophilus protein · the same entry in another collection · chain A against A, TM-score 1.00
- P84138 · AlphaFold monomer V2.0 prediction for purine nucleoside phosphorylase ylmd (P84138) · 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 P84138
- Elsewhere: RCSB PDB 1T8H · PDBe 1T8H · UniProt P84138
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.