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Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase from Amycolatopsis mediterranei (AmGH128_I) in complex with laminaritriose

Analyse Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UAR
Type: protein
Length: 241 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.4
Source: Amycolatopsis mediterranei
Molecule: Glyco_hydro_cc domain-containing protein
UniProt: G0FQ07
Ligands: BGC
Pockets: 1 · best druggability 0.25

Structure

x-ray diffraction · resolution 1.4 · 1 distinct chain · 36% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glyco_hydro_cc domain-containing protein	protein	241	36% helix, 20% strand	G0FQ07

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 3 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	56	0.25	0.72	17	BGC

Compared structures

6UAR · Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase from amycolatopsis… · 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 G0FQ07
Elsewhere: RCSB PDB 6UAR · PDBe 6UAR · UniProt G0FQ07

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