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Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E102A mutant) from amycolatopsis mediterranei (AMGH128_I) in complex with laminaripentaose

Analyse Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E102A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UAT
Type: protein
Length: 241 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GLYCO_HYDRO_CC domain-containing protein
UniProt: G0FQ07
Ligands: BGC, ZN
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · 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 · 5 copies · chains A
ZN · Zinc ion · metal · 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	79	0.33	0.74	19	BGC

Compared structures

6UAT · Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase (E102A mutant) from… · 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 6UAT · PDBe 6UAT · UniProt G0FQ07

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