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Crystal structure of a GH128 (subgroup III) curdlan-specific exo-beta- 1,3-glucanase from blastomyces gilchristii (BGGH128_III)

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: 6UAY
Type: protein
Length: 482 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoside hydrolase
UniProt: A0A179UGT5
Pockets: 4 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycoside hydrolase	protein	238	39% helix, 21% strand	A0A179UGT5
B	Glycoside hydrolase	protein	244	40% helix, 21% strand	A0A179UGT5

Pockets

4 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	558	0.69	0.79	72	empty
2	71	0.36	0.77	19	empty
3	58	0.34	0.77	19	empty
4	76	0.33	0.75	22	empty

Interfaces

1 interface between chains.

A–B · 392 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

6UAY · 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

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Every structure of UniProt A0A179UGT5
Elsewhere: RCSB PDB 6UAY · PDBe 6UAY · UniProt A0A179UGT5

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