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Fmo protein from prosthecochloris aestuarii 2K at room temperature

Analyse Fmo protein from prosthecochloris aestuarii 2K at room temperature in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BCL
Type: protein
Length: 350 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bacteriochlorophyll a protein
UniProt: P11741
Ligands: BCL
Pockets: 3 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bacteriochlorophyll a protein	protein	350	17% helix, 49% strand	P11741

Ligands and binding sites

BCL · Bacteriochlorophyll A · ligand · 7 copies · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	925	0.81	0.82	92	BCL
2	223	0.65	0.82	25	BCL
3	131	0.51	0.79	23	BCL

Compared structures

4BCL · FMO protein from Prosthecochloris aestuarii 2K at Room Temperature · the same entry in another collection · chain A against A, TM-score 1.00
P11741 · AlphaFold monomer V2.0 prediction for bacteriochlorophyll a protein (P11741) · a predicted model of the same protein · 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 P11741
Elsewhere: RCSB PDB 4BCL · PDBe 4BCL · UniProt P11741

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