Research workbench
Structure of klebsiella pneumoniae 5-hydroxyisourate hydrolase
Analyse Structure of klebsiella pneumoniae 5-hydroxyisourate hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QVA
- Type
- protein
- Length
- 422 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transthyretin-like protein
- UniProt
- A6T926
- Ligands
- PO4
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 4 distinct chains · 7% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transthyretin-like protein | protein | 109 | 6% helix, 49% strand | A6T926 |
| B | Transthyretin-like protein | protein | 105 | 7% helix, 53% strand | A6T926 |
| C | Transthyretin-like protein | protein | 105 | 7% helix, 53% strand | A6T926 |
| D | Transthyretin-like protein | protein | 103 | 7% helix, 52% strand | A6T926 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains B, C, A, D
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 | 118 | 0.79 | 0.98 | 30 | empty |
| 2 | 74 | 0.35 | 0.77 | 22 | PO4 |
Interfaces
6 interfaces between chains.
- A–B · 882 Ų buried · 20 hydrogen bonds · protein-protein
- C–D · 876 Ų buried · 20 hydrogen bonds · protein-protein
- A–D · 446 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 407 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 249 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 3QVA · Structure of Klebsiella pneumoniae 5-hydroxyisourate hydrolase · 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 A6T926
- Elsewhere: RCSB PDB 3QVA · PDBe 3QVA · UniProt A6T926
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