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Apo mouse acidic mammalian chitinase, catalytic domain at 100 K

Analyse Apo mouse acidic mammalian chitinase, catalytic domain at 100 K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8FG5
Type: protein
Length: 376 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.3
Source: Mus musculus
Molecule: Acidic mammalian chitinase
EC: 3.2.1.14
UniProt: Q91XA9
Ligands: MG
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · resolution 1.3 · 1 distinct chain · 37% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Acidic mammalian chitinase (EC 3.2.1.14)	protein	376	37% helix, 22% strand	Q91XA9

Ligands and binding sites

MG · Magnesium ion · metal · 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	447	0.62	0.76	47	MG

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

Q91XA9 · AlphaFold monomer V2.0 prediction for acidic mammalian chitinase (Q91XA9) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q91XA9
Elsewhere: RCSB PDB 8FG5 · PDBe 8FG5 · UniProt Q91XA9

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