MolNFT v1 · #102814 · protein
Structure of synechococcus elongatus pcc 7942 CCMK2
4OX7 · Carbon dioxide-concentrating mechanism protein ccmk: “Structure of synechococcus elongatus pcc 7942 CCMK2”. X-ray diffraction, 1 pocket (best druggability 0.47). MolNFT v1 #102814 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4OX7
- Type
- protein
- Length
- 606 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbon dioxide-concentrating mechanism protein ccmk
- UniProt
- Q03511
- Pockets
- 1 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Carbon dioxide-concentrating mechanism protein ccmk | protein | 101 | 38% helix, 33% strand | Q03511 |
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 | 236 | 0.47 | 0.73 | 24 | empty |
Interfaces
6 interfaces between chains.
- A–F · 1144 Ų buried · 12 hydrogen bonds · protein-protein
- D–E · 1140 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 1134 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 1134 Ų buried · 12 hydrogen bonds · protein-protein
- E–F · 1134 Ų buried · 11 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 Q03511
- Elsewhere: RCSB PDB 4OX7 · PDBe 4OX7 · UniProt Q03511
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