Research workbench

Crystal structure of acidovorax avenae L-fucose mutarotase (apo form)

Analyse Crystal structure of acidovorax avenae L-fucose mutarotase (apo form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BYU
Type: protein
Length: 216 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-fucose mutarotase
UniProt: F0Q4R9
Ligands: 1PG
Pockets: 2 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	L-fucose mutarotase	protein	108	40% helix, 32% strand	F0Q4R9

Ligands and binding sites

1PG · 2-(2-{2-[2-(2-methoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethanol · ligand · 2 copies · chains A, B
EDO · 1,2-ethanediol · additive · 2 copies · chains A, B

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

Pockets

2 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	247	0.66	0.83	27	1PG, EDO
2	286	0.65	0.81	34	1PG, EDO

Interfaces

1 interface between chains.

A–B · 1754 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

7BYU · Crystal structure of Acidovorax avenae L-fucose mutarotase (apo form) · 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 F0Q4R9
Elsewhere: RCSB PDB 7BYU · PDBe 7BYU · UniProt F0Q4R9

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.