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Crystal structure of 5-hydroxyisourate hydrolase (formerly known as TRP, transthyretin related protein)
Analyse Crystal structure of 5-hydroxyisourate hydrolase (formerly known as TRP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2H1X
- Type
- protein
- Length
- 452 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5-hydroxyisourate hydrolase (formerly known as TRP, transthyretin related protein)
- EC
- 3.5.2.17
- UniProt
- Q0P422
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | 5-hydroxyisourate hydrolase (formerly known as TRP, transthyretin related protein) (EC 3.5.2.17) | protein | 113 | 5% helix, 43% strand | Q0P422 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.79 | 0.98 | 29 | empty |
| 2 | 63 | 0.39 | 0.80 | 17 | empty |
| 3 | 73 | 0.36 | 0.78 | 23 | empty |
| 4 | 53 | 0.27 | 0.74 | 13 | empty |
Interfaces
6 interfaces between chains.
- A–B · 930 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 928 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 406 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 391 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 299 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 2H1X · Crystal structure of 5-hydroxyisourate Hydrolase (formerly known as TRP, Transthyretin… · 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 Q0P422
- Elsewhere: RCSB PDB 2H1X · PDBe 2H1X · UniProt Q0P422
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