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
- 4CF5
- Type
- protein
- Length
- 901 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-haloacid dehalogenase
- EC
- 3.8.1.2
- UniProt
- M9P6K0
- Pockets
- 8 · best druggability 0.61
Structure
x-ray diffraction · 4 distinct chains · 49% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-haloacid dehalogenase (EC 3.8.1.2) | protein | 223 | 49% helix, 14% strand | M9P6K0 |
| B | L-haloacid dehalogenase (EC 3.8.1.2) | protein | 228 | 50% helix, 13% strand | M9P6K0 |
| C | L-haloacid dehalogenase (EC 3.8.1.2) | protein | 226 | 49% helix, 13% strand | M9P6K0 |
| D | L-haloacid dehalogenase (EC 3.8.1.2) | protein | 224 | 47% helix, 13% strand | M9P6K0 |
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 199 | 0.61 | 0.82 | 36 | empty |
| 2 | 192 | 0.57 | 0.80 | 30 | empty |
| 3 | 186 | 0.56 | 0.80 | 32 | empty |
| 4 | 161 | 0.55 | 0.80 | 25 | empty |
| 5 | 127 | 0.46 | 0.78 | 25 | empty |
Interfaces
2 interfaces between chains.
- C–D · 1955 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 1933 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (nonstandard).
Compared structures
- 4CF5 · 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 4CF5 · PDBe 4CF5 · UniProt M9P6K0
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