MolNFT v1 · #16202 · protein
The structure of a haloacid dehalogenase-like hydrolase from B. subtilis
1NRW · Hypothetical protein, haloacid dehalogenase-like hydrolase: “The structure of a haloacid dehalogenase-like hydrolase from B. subtilis”. X-ray diffraction, 2 ligands (CA, PO4), 3 pockets (best druggability 0.49). MolNFT v1 #16202 on…
- PDB
- 1NRW
- Type
- protein
- Length
- 285 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein, haloacid dehalogenase-like hydrolase
- UniProt
- P94592
- Ligands
- CA, PO4
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein, haloacid dehalogenase-like hydrolase | protein | 285 | 45% helix, 21% strand | P94592 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 81 | 0.49 | 0.83 | 27 | PO4 |
| 2 | 72 | 0.30 | 0.73 | 21 | empty |
| 3 | 57 | 0.30 | 0.75 | 14 | empty |
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 1NRW · The structure of a HALOACID DEHALOGENASE-LIKE HYDROLASE FROM B. SUBTILIS · the same entry in another collection · chain A against A, TM-score 1.00
- P94592 · AlphaFold monomer V2.0 prediction for phosphatase ywpj (P94592) · 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 P94592
- Elsewhere: RCSB PDB 1NRW · PDBe 1NRW · UniProt P94592
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