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Crystal structure of a putative glycosyl hydrolase (BACUNI_00951) from bacteroides uniformis atcc 8492 at 2.15 a resolution

Analyse Crystal structure of a putative glycosyl hydrolase (BACUNI_00951) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HXC
Type: protein
Length: 255 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative glycosyl hydrolase
UniProt: A7V066
Pockets: 3 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative glycosyl hydrolase	protein	255	10% helix, 40% strand	A7V066

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 3 copies · chains A
PGE · Triethylene glycol · additive · chains A
PEG · Di(hydroxyethyl)ether · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	95	0.65	0.90	22	PGE
2	67	0.35	0.77	19	empty
3	56	0.31	0.76	16	empty

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

4HXC · Crystal structure of a putative glycosyl hydrolase (BACUNI_00951) from Bacteroides… · 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 A7V066
Elsewhere: RCSB PDB 4HXC · PDBe 4HXC · UniProt A7V066

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