Research workbench
Crystal structure of cprk C200S
Analyse Crystal structure of cprk C200S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3E6D
- Type
- protein
- Length
- 405 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclic nucleotide-binding protein
- UniProt
- Q18R04
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclic nucleotide-binding protein | protein | 202 | 41% helix, 30% strand | Q18R04 |
| B | Cyclic nucleotide-binding protein | protein | 203 | 41% helix, 27% strand | Q18R04 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 125 | 0.71 | 0.91 | 34 | empty |
| 2 | 212 | 0.68 | 0.85 | 42 | empty |
| 3 | 282 | 0.52 | 0.75 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 2522 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 3E6D · Crystal Structure of CprK C200S · 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 Q18R04
- Elsewhere: RCSB PDB 3E6D · PDBe 3E6D · UniProt Q18R04
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