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Crystal structure of native chitosanase from Bacillus subtilis MY002

Analyse Crystal structure of native chitosanase from Bacillus subtilis MY002 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7C6C
Type: protein
Length: 241 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.258
Source: Bacillus subtilis subsp. subtilis str. 168
Molecule: Chitosanase
EC: 3.2.1.132
UniProt: O07921
Ligands: LMR
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · resolution 1.258 · 1 distinct chain · 57% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chitosanase (EC 3.2.1.132)	protein	241	57% helix, 7% strand	O07921

Ligands and binding sites

LMR · (2S)-2-hydroxybutanedioic acid · ligand · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	291	0.64	0.81	46	empty

Compared structures

7C6C · Crystal structure of native chitosanase from bacillus subtilis MY002 · the same entry in another collection · chain A against A, TM-score 1.00
O07921 · AlphaFold monomer V2.0 prediction for chitosanase (O07921) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 O07921
Elsewhere: RCSB PDB 7C6C · PDBe 7C6C · UniProt O07921

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