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Crystal structure of 4-nitrophenylphosphatase (TM1742) from thermotoga maritima at 2.40 a resolution
Analyse Crystal structure of 4-nitrophenylphosphatase (TM1742) from thermotoga maritima… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VJR
- Type
- protein
- Length
- 261 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-nitrophenylphosphatase
- EC
- 3.1.3.41
- UniProt
- Q9X264
- Ligands
- NI, CL
- Pockets
- 2 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-nitrophenylphosphatase (EC 3.1.3.41) | protein | 261 | 42% helix, 20% strand | Q9X264 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.60 | 0.82 | 34 | empty |
| 2 | 99 | 0.34 | 0.73 | 16 | empty |
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 1VJR · Crystal structure of 4-nitrophenylphosphatase (TM1742) from Thermotoga maritima at 2.40 A… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9X264
- Elsewhere: RCSB PDB 1VJR · PDBe 1VJR · UniProt Q9X264
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