MolNFT v1 · #62104 · protein
Unbound oxidised cprk
3E5Q · Cyclic nucleotide-binding protein: “Unbound oxidised cprk”. X-ray diffraction, 14 pockets (best druggability 0.75). MolNFT v1 #62104 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3E5Q
- Type
- protein
- Length
- 1,213 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclic nucleotide-binding protein
- UniProt
- Q18R04
- Pockets
- 14 · best druggability 0.75
Structure
x-ray diffraction · 4 distinct chains · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclic nucleotide-binding protein | protein | 202 | 38% helix, 22% strand | Q18R04 |
| B, D | Cyclic nucleotide-binding protein | protein | 201 | 38% helix, 28% strand | Q18R04 |
| C, E | Cyclic nucleotide-binding protein | protein | 203 | 34% helix, 24% strand | Q18R04 |
| F | Cyclic nucleotide-binding protein | protein | 203 | 38% helix, 28% strand | Q18R04 |
Pockets
14 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 157 | 0.75 | 0.92 | 39 | empty |
| 2 | 190 | 0.72 | 0.89 | 36 | empty |
| 3 | 130 | 0.70 | 0.90 | 35 | empty |
| 4 | 99 | 0.69 | 0.92 | 24 | empty |
| 5 | 100 | 0.66 | 0.90 | 25 | empty |
Interfaces
5 interfaces between chains.
- E–F · 2490 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 2447 Ų buried · 21 hydrogen bonds · protein-protein
- C–D · 2444 Ų buried · 24 hydrogen bonds · protein-protein
- A–E · 333 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 326 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3E5Q · Unbound Oxidised CprK · 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 3E5Q · PDBe 3E5Q · UniProt Q18R04
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