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Crystal structure of putative glycosyl hydrolase, was domain of unknown function (DUF1080) (YP_001302580.1) from parabacteroides distasonis atcc 8503 at 2.36 a resolution

Analyse Crystal structure of putative glycosyl hydrolase, was domain of unknown… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HBK
Type: protein
Length: 231 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative glycosyl hydrolase
UniProt: A6LB94
Ligands: SO4
Pockets: 1 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative glycosyl hydrolase	protein	231	9% helix, 34% strand	A6LB94

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 4 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	120	0.39	0.75	29	SO4, EDO

Modifications

Observed in the structure: 1 modified (engineered).

Compared structures

3HBK · Crystal structure of putative glycosyl hydrolase, was Domain of Unknown Function… · 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 A6LB94
Elsewhere: RCSB PDB 3HBK · PDBe 3HBK · UniProt A6LB94

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