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The crystal structure of light-driven chloride pump ClR (T102D) mutant at pH 4.5.
Analyse The crystal structure of light-driven chloride pump ClR (T102D) mutant at pH… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5G2C
- Type
- protein
- Length
- 268 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.31
- Source
- NONLABENS MARINUS S1-08
- Molecule
- Chloride pumping rhodopsin
- UniProt
- W8VZW3
- Ligands
- OLA, RET, CL
- Pockets
- 1 · best druggability 0.72
Structure
x-ray diffraction · resolution 2.31 · 1 distinct chain · 81% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chloride pumping rhodopsin | protein | 268 | 81% helix, 3% strand | W8VZW3 |
Ligands and binding sites
- OLA · Oleic acid · ligand · 8 copies · chains A
- RET · Retinal · ligand · chains A
- CL · Chloride ion · ion · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 129 | 0.72 | 0.91 | 23 | RET |
Modifications
Observed in the structure: 1 cofactor (retinal Schiff base).
Compared structures
- 5G2C · The crystal structure of light-driven chloride pump clr (T102D) mutant at pH 4.5. · 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 W8VZW3
- Elsewhere: RCSB PDB 5G2C · PDBe 5G2C · UniProt W8VZW3
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