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Crystal stricture of D143A chitinase in complex with nag from bacillus cereus NCTU2

Analyse Crystal stricture of D143A chitinase in complex with nag from bacillus cereus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3N13
Type: protein
Length: 326 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chitinase a
EC: 3.2.1.14
UniProt: D0VV09
Ligands: NAG
Pockets: 2 · best druggability 0.44

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chitinase a (EC 3.2.1.14)	protein	326	35% helix, 22% strand	D0VV09

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	155	0.44	0.75	25	NAG
2	54	0.32	0.77	18	empty

Compared structures

3N13 · Crystal stricture of D143A chitinase in complex with NAG from Bacillus cereus NCTU2 · 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 D0VV09
Elsewhere: RCSB PDB 3N13 · PDBe 3N13 · UniProt D0VV09

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