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Crystal structure of cruxrhodopsin-3 at PH5 from haloarcula vallismortis at 2.1 ångström resolution

Analyse Crystal structure of cruxrhodopsin-3 at PH5 from haloarcula vallismortis at 2.1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4L35
Type: protein
Length: 244 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cruxrhodopsin-3
UniProt: P94854
Ligands: RET, 22B
Pockets: 1 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 73% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cruxrhodopsin-3	protein	244	73% helix, 5% strand	P94854

Ligands and binding sites

RET · Retinal · ligand · chains A
22B · Bacterioruberin · ligand · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	123	0.80	0.98	25	RET

Modifications

Observed in the structure: 1 cofactor (retinal Schiff base).

Compared structures

4L35 · Crystal structure of cruxrhodopsin-3 at pH5 from Haloarcula vallismortis at 2.1 angstrom… · the same entry in another collection · chain A against A, TM-score 1.00
P94854 · AlphaFold monomer V2.0 prediction for cruxrhodopsin-3 (P94854) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P94854
Elsewhere: RCSB PDB 4L35 · PDBe 4L35 · UniProt P94854

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