Research workbench
Crystal structure of reduced cprk in absence of any ligand
Analyse Crystal structure of reduced cprk in absence of any ligand in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2H6C
- Type
- protein
- Length
- 416 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chlorophenol reduction gene K
- UniProt
- Q9LAS2
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Chlorophenol reduction gene K | protein | 208 | 39% helix, 26% strand | Q9LAS2 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 112 | 0.75 | 0.95 | 22 | empty |
| 2 | 127 | 0.70 | 0.91 | 28 | empty |
| 3 | 240 | 0.52 | 0.76 | 31 | empty |
| 4 | 165 | 0.48 | 0.76 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 2878 Ų buried · 34 hydrogen bonds · protein-protein
Compared structures
- 2H6C · Crystal structure of reduced CprK in absence of any ligand · 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 Q9LAS2
- Elsewhere: RCSB PDB 2H6C · PDBe 2H6C · UniProt Q9LAS2
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