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Crystal structure of a GH128 (subgroup III) curdlan-specific exo-beta- 1,3-glucanase from blastomyces gilchristii (BGGH128_III) in complex with laminaribiose at -2 and -1 subsites

Analyse Crystal structure of a GH128 (subgroup III) curdlan-specific exo-beta… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UB0
Type: protein
Length: 230 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GLYCO_HYDRO_CC domain-containing protein
UniProt: A0A179UGT5
Ligands: GLC, BGC
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GLYCO_HYDRO_CC domain-containing protein	protein	230	41% helix, 22% strand	A0A179UGT5

Ligands and binding sites

GLC · alpha-D-glucopyranose · sugar · chains A
BGC · beta-D-glucopyranose · sugar · 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	62	0.35	0.77	20	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

6UB0 · Crystal structure of a GH128 (subgroup III) curdlan-specific exo-beta-1,3-glucanase 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 A0A179UGT5
Elsewhere: RCSB PDB 6UB0 · PDBe 6UB0 · UniProt A0A179UGT5

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