Research workbench
Mutagenesis of a rhodobacteraceae L-haloacid dehalogenase
Analyse Mutagenesis of a rhodobacteraceae L-haloacid dehalogenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CF4
- Type
- protein
- Length
- 446 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-haloacid dehalogenase
- EC
- 3.8.1.2
- UniProt
- M9P6K0
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | L-haloacid dehalogenase (EC 3.8.1.2) | protein | 223 | 49% helix, 14% strand | M9P6K0 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 194 | 0.57 | 0.80 | 29 | empty |
| 2 | 187 | 0.55 | 0.79 | 29 | empty |
| 3 | 106 | 0.41 | 0.77 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1904 Ų buried · 27 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 4CF4 · Mutagenesis of a Rhodobacteraceae L-haloacid dehalogenase · 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 M9P6K0
- Elsewhere: RCSB PDB 4CF4 · PDBe 4CF4 · UniProt M9P6K0
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