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Crystal structure of the chlamydomonas reinhardtii LCI1 channel

Analyse Crystal structure of the chlamydomonas reinhardtii LCI1 channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6BHP
Type
protein
Length
510 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Membrane protein
UniProt
Q39583
Ligands
HG, CO2
Pockets
9 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 81% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CMembrane proteinprotein17081% helix, 0% strandQ39583

Ligands and binding sites

  • HG · Mercury (II) ion · metal · 3 copies · chains A, B, C
  • CO2 · Carbon dioxide · ion · chains C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1980.730.9427empty
22750.660.8232empty
3760.620.8916empty
42370.520.7629empty
51810.510.7720empty

Interfaces

3 interfaces between chains.

  • B–C · 1146 Ų buried · 15 hydrogen bonds · protein-protein
  • A–B · 1130 Ų buried · 9 hydrogen bonds · protein-protein
  • A–C · 989 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 6BHP · Crystal structure of the Chlamydomonas reinhardtii LCI1 channel · the same entry in another collection · chain A against A, TM-score 1.00

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