Research workbench
Wild-type pseudomonas fluorescens isocyanide hydratase (wt-2) at 274K, phenix-refined
Analyse Wild-type pseudomonas fluorescens isocyanide hydratase (wt-2) at 274K… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LBI
- Type
- protein
- Length
- 456 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isonitrile hydratase inha
- UniProt
- Q4K977
- Pockets
- 4 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isonitrile hydratase inha | protein | 226 | 43% helix, 19% strand | Q4K977 |
| B | Isonitrile hydratase inha | protein | 230 | 42% helix, 20% strand | Q4K977 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 243 | 0.58 | 0.79 | 27 | empty |
| 2 | 231 | 0.58 | 0.79 | 25 | empty |
| 3 | 61 | 0.34 | 0.77 | 18 | empty |
| 4 | 62 | 0.29 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2550 Ų buried · 41 hydrogen bonds · protein-protein
Compared structures
- 7LBI · Wild-type Pseudomonas fluorescens isocyanide hydratase (WT-2) at 274K, PHENIX-refined · 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 Q4K977
- Elsewhere: RCSB PDB 7LBI · PDBe 7LBI · UniProt Q4K977
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.