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Crystal structure of a plant class V chitinase mutant from cycas revoluta in complex with (GLCNAC)3

Analyse Crystal structure of a plant class V chitinase mutant from cycas revoluta in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WIJ
Type: protein
Length: 340 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chitinase a
EC: 3.2.1.14
UniProt: Q4W6L6
Ligands: NAG
Pockets: 1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chitinase a (EC 3.2.1.14)	protein	340	39% helix, 26% strand	Q4W6L6

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
ACT · Acetate ion · additive · 2 copies · 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	192	0.48	0.75	42	NAG, ACT

Compared structures

3WIJ · Crystal structure of a plant class V chitinase mutant from Cycas revoluta in complex with… · 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 3WIJ · PDBe 3WIJ · UniProt Q4W6L6

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