Research workbench
Cobalt transporter ATP-binding subunit
Analyse Cobalt transporter ATP-binding subunit in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MKI
- Type
- protein
- Length
- 568 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.3
- Source
- Thermoanaerobacter tengcongensis
- Molecule
- Energy-coupling factor transporter ATP-binding protein EcfA2
- EC
- 3.6.3.-
- UniProt
- Q8R7Y5
- Ligands
- SO4
- Pockets
- 6 · best druggability 0.78
Structure
x-ray diffraction · resolution 2.3 · 2 distinct chains · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Energy-coupling factor transporter ATP-binding protein EcfA2 (EC 3.6.3.-) | protein | 283 | 43% helix, 22% strand | Q8R7Y5 |
| A | Energy-coupling factor transporter ATP-binding protein EcfA2 (EC 3.6.3.-) | protein | 285 | 42% helix, 21% strand | Q8R7Y5 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains B, A
- LMT · Dodecyl-beta-D-maltoside · additive · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1142 | 0.78 | 0.80 | 106 | SO4, LMT |
| 2 | 233 | 0.61 | 0.80 | 23 | empty |
| 3 | 152 | 0.61 | 0.84 | 22 | LMT |
| 4 | 195 | 0.59 | 0.81 | 25 | empty |
| 5 | 67 | 0.44 | 0.81 | 12 | empty |
Interfaces
1 interface between chains.
- B–A · 1520 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 Q8R7Y5
- Elsewhere: RCSB PDB 4MKI · PDBe 4MKI · UniProt Q8R7Y5
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