Research workbench

Crystal Structure of GH18 Chitinase from Cycas revoluta in complex with (GlcNAc)3

Analyse Crystal Structure of GH18 Chitinase from Cycas revoluta in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MNK
Type: protein
Length: 342 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.29
Source: Cycas revoluta
Molecule: Chitinase A
EC: 3.2.1.14
UniProt: Q4W6L6
Ligands: NAG
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · resolution 1.29 · 1 distinct chain · 38% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chitinase A (EC 3.2.1.14)	protein	342	38% helix, 26% strand	Q4W6L6

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
ACT · Acetate ion · additive · chains A
B3P · 2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-propane-1,3-diol · additive · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	161	0.50	0.77	32	NAG

Compared structures

4MNK · Crystal structure of GH18 chitinase from cycas revoluta in complex with (GLCNAC)3 · 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 Q4W6L6
Elsewhere: RCSB PDB 4MNK · PDBe 4MNK · UniProt Q4W6L6

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