Research workbench
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
- 2H6U
- Type
- protein
- Length
- 912 residues
- Chains
- 8
- 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
- 7 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | 5-hydroxyisourate hydrolase (formerly known as TRP, transthyretin related protein) (EC 3.5.2.17) | protein | 114 | 6% helix, 43% strand | Q0P422 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 112 | 0.80 | 0.99 | 28 | empty |
| 2 | 111 | 0.79 | 0.98 | 28 | empty |
| 3 | 959 | 0.75 | 0.78 | 68 | empty |
| 4 | 124 | 0.49 | 0.80 | 41 | empty |
| 5 | 107 | 0.49 | 0.81 | 33 | empty |
Interfaces
15 interfaces between chains.
- E–F · 924 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 919 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 917 Ų buried · 10 hydrogen bonds · protein-protein
- G–H · 911 Ų buried · 10 hydrogen bonds · protein-protein
- B–F · 405 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2H6U · Crystal structure of 5-hydroxyisourate hydrolase (formerly known as TRP, transthyretin… · the same entry in another collection · chain B against B, 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 2H6U · PDBe 2H6U · UniProt Q0P422
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