Research workbench
Crystal structure of hypothetical protein PH1421 from pyrococcus horikoshii.
Analyse Crystal structure of hypothetical protein PH1421 from pyrococcus horikoshii. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WR8
- Type
- protein
- Length
- 461 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoglycolate phosphatase
- EC
- 3.1.3.18
- UniProt
- O50129
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoglycolate phosphatase (EC 3.1.3.18) | protein | 230 | 41% helix, 20% strand | O50129 |
| B | Phosphoglycolate phosphatase (EC 3.1.3.18) | protein | 231 | 42% helix, 19% strand | O50129 |
Ligands and binding sites
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 488 | 0.70 | 0.80 | 63 | empty |
| 2 | 421 | 0.67 | 0.80 | 53 | ACT |
Interfaces
1 interface between chains.
- A–B · 1259 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 1WR8 · Crystal structure of hypothetical protein PH1421 from Pyrococcus horikoshii. · the same entry in another collection · chain A against A, TM-score 1.00
- O50129 · AlphaFold monomer V2.0 prediction for phosphoglycolate phosphatase (O50129) · 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 O50129
- Elsewhere: RCSB PDB 1WR8 · PDBe 1WR8 · UniProt O50129
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