Research workbench

Comparison of family 12 glycoside hydrolases and recruited substitutions important for thermal stability

Analyse Comparison of family 12 glycoside hydrolases and recruited substitutions… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1OA4
Type: protein
Length: 222 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-beta-1,4-glucanase
EC: 3.2.1.4
UniProt: Q9KIH1
Pockets: 1 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-beta-1,4-glucanase (EC 3.2.1.4)	protein	222	6% helix, 50% strand	Q9KIH1

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	193	0.57	0.80	42	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1OA4 · Comparison of Family 12 Glycoside Hydrolases and Recruited Substitutions Important for… · 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 Q9KIH1
Elsewhere: RCSB PDB 1OA4 · PDBe 1OA4 · UniProt Q9KIH1

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.