Research workbench
Crystal structure of AFCBBQ2, a moxr aaa+-ATPase and cbbqo-type rubisco activase from acidithiobacillus ferrooxidans
Analyse Crystal structure of AFCBBQ2, a moxr aaa+-ATPase and cbbqo-type rubisco… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L1Q
- Type
- protein
- Length
- 801 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cbbq protein
- UniProt
- B7J5E4
- Ligands
- ADP, PO4
- Pockets
- 11 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, A, B | Cbbq protein | protein | 267 | 43% helix, 16% strand | B7J5E4 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 3 copies · chains C, A, B
- PO4 · Phosphate ion · ion · 3 copies · chains C, A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 536 | 0.80 | 0.86 | 59 | ADP, PO4 |
| 2 | 93 | 0.69 | 0.92 | 18 | empty |
| 3 | 142 | 0.59 | 0.84 | 17 | ADP |
| 4 | 175 | 0.59 | 0.82 | 26 | ADP, PO4 |
| 5 | 268 | 0.56 | 0.77 | 37 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2168 Ų buried · 40 hydrogen bonds · protein-protein
- C–B · 212 Ų buried · 3 hydrogen bonds · protein-protein
- C–A · 123 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6L1Q · Crystal structure of AfCbbQ2, a MoxR AAA+-ATPase and CbbQO-type Rubisco activase from… · 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 B7J5E4
- Elsewhere: RCSB PDB 6L1Q · PDBe 6L1Q · UniProt B7J5E4
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