Research workbench

Catalytic domain of chitinase A1 from bacillus circulans wl-12

Analyse Catalytic domain of chitinase A1 from bacillus circulans wl-12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ITX
Type: protein
Length: 419 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycosyl hydrolase
EC: 3.2.1.14
UniProt: P20533
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycosyl hydrolase (EC 3.2.1.14)	protein	419	35% helix, 22% strand	P20533

Ligands and binding sites

GOL · Glycerol · additive · 11 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 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	582	0.72	0.80	51	GOL
2	61	0.38	0.79	14	empty
3	52	0.25	0.73	17	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1ITX · Catalytic Domain of Chitinase A1 from Bacillus circulans WL-12 · the same entry in another collection · chain A against A, TM-score 1.00
P20533 · AlphaFold monomer V2.0 prediction for chitinase A1 (P20533) · a predicted model of the same protein · 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 P20533
Elsewhere: RCSB PDB 1ITX · PDBe 1ITX · UniProt P20533

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