MolNFT v1 · #2264 · protein

Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy

1BRD · Bacteriorhodopsin precursor: “Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy”. Electron crystallography, 1 ligand (RET), 3 pockets (best druggability 0.75). MolNFT v1 #2264 on…

PDB: 1BRD
Type: protein
Length: 170 residues
Chains: 1
Method: electron crystallography
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bacteriorhodopsin precursor
UniProt: P02945
Ligands: RET
Pockets: 3 · best druggability 0.75

Structure

electron crystallography · 1 distinct chain · 92% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bacteriorhodopsin precursor	protein	170	92% helix, 0% strand	P02945

Ligands and binding sites

RET · Retinal · ligand · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	123	0.75	0.94	24	RET
2	109	0.51	0.81	25	empty
3	93	0.48	0.81	23	empty

Modifications

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

Compared structures

1BRD · Model for the structure of Bacteriorhodopsin based on high-resolution Electron… · the same entry in another collection · chain A against A, TM-score 1.00
P02945 · AlphaFold monomer V2.0 prediction for bacteriorhodopsin (P02945) · a predicted model of the same protein · chain A against A, TM-score 0.91

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 P02945
Elsewhere: RCSB PDB 1BRD · PDBe 1BRD · UniProt P02945

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