Research workbench
Haloalkane dehalogenase mutant with phe 172 replaced with TRP
Analyse Haloalkane dehalogenase mutant with phe 172 replaced with TRP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HDE
- Type
- protein
- Length
- 620 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Haloalkane dehalogenase
- EC
- 3.8.1.5
- UniProt
- P22643
- Pockets
- 3 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Haloalkane dehalogenase (EC 3.8.1.5) | protein | 310 | 45% helix, 17% strand | P22643 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.39 | 0.79 | 18 | empty |
| 2 | 120 | 0.38 | 0.74 | 14 | empty |
| 3 | 69 | 0.28 | 0.72 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 189 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
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 P22643
- Elsewhere: RCSB PDB 1HDE · PDBe 1HDE · UniProt P22643
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