MolNFT v1 · #125018 · protein
Thermostable mutant of halohydrin dehalogenase hhec - C153N
5KWE: “Thermostable mutant of halohydrin dehalogenase hhec - C153N”. X-ray diffraction, 2 ligands (NA, CL), 10 pockets (best druggability 0.86). MolNFT v1 #125018 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5KWE
- Type
- protein
- Length
- 1,019 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Halohydrin dehalogenase
- UniProt
- Q93D82
- Ligands
- NA, CL
- Pockets
- 10 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D | Halohydrin dehalogenase | protein | 255 | 49% helix, 14% strand | Q93D82 |
| B | Halohydrin dehalogenase | protein | 254 | 49% helix, 15% strand | Q93D82 |
Ligands and binding sites
- NA · Sodium ion · metal · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · 5 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 962 | 0.86 | 0.87 | 87 | empty |
| 2 | 117 | 0.54 | 0.82 | 30 | empty |
| 3 | 104 | 0.50 | 0.82 | 20 | empty |
| 4 | 97 | 0.50 | 0.82 | 15 | empty |
| 5 | 98 | 0.48 | 0.81 | 16 | empty |
Interfaces
6 interfaces between chains.
- B–C · 1723 Ų buried · 19 hydrogen bonds · protein-protein
- A–D · 1721 Ų buried · 19 hydrogen bonds · protein-protein
- C–D · 1547 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 1544 Ų buried · 25 hydrogen bonds · protein-protein
- A–C · 1241 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 5KWE · Thermostable mutant of halohydrin dehalogenase HheC - C153N · 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 Q93D82
- Elsewhere: RCSB PDB 5KWE · PDBe 5KWE · UniProt Q93D82
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.