MolNFT v1 · #102815 · protein
Structure of prochlorococcus marinus str. mit 9313 CSOS1
4OX8 · Carbon dioxide-concentrating mechanism protein ccmk: “Structure of prochlorococcus marinus str. mit 9313 CSOS1”. X-ray diffraction, 1 pocket (best druggability 0.32). MolNFT v1 #102815 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4OX8
- Type
- protein
- Length
- 525 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbon dioxide-concentrating mechanism protein ccmk
- UniProt
- Q7V6F7
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbon dioxide-concentrating mechanism protein ccmk | protein | 90 | 40% helix, 36% strand | Q7V6F7 |
| B, C, D, E, F | Carbon dioxide-concentrating mechanism protein ccmk | protein | 87 | 40% helix, 37% strand | Q7V6F7 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.32 | 0.73 | 23 | empty |
Interfaces
6 interfaces between chains.
- C–D · 946 Ų buried · 10 hydrogen bonds · protein-protein
- E–F · 934 Ų buried · 10 hydrogen bonds · protein-protein
- B–F · 932 Ų buried · 10 hydrogen bonds · protein-protein
- D–E · 929 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 922 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
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 Q7V6F7
- Elsewhere: RCSB PDB 4OX8 · PDBe 4OX8 · UniProt Q7V6F7
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.