MolNFT v1 · #125105 · protein

1.25 ångström crystal structure of chitinase from bacillus anthracis.

5KZ6: “1.25 ångström crystal structure of chitinase from bacillus anthracis.”. X-ray diffraction, 3 ligands (ZN, NA, CL), 6 pockets (best druggability 0.85). MolNFT v1 #125105 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5KZ6
Type: protein
Length: 654 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chitinase
UniProt: Q81WW1
Ligands: ZN, NA, CL
Pockets: 6 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Chitinase	protein	327	35% helix, 21% strand	Q81WW1

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B
NA · Sodium ion · metal · 3 copies · chains A, B
CL · Chloride ion · ion · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	823	0.85	0.88	60	ZN
2	495	0.65	0.77	58	empty
3	231	0.49	0.75	36	empty
4	55	0.29	0.75	13	empty
5	62	0.29	0.74	19	empty

Interfaces

1 interface between chains.

A–B · 1091 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

5KZ6 · 1.25 Angstrom Crystal Structure of Chitinase from Bacillus anthracis. · 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 Q81WW1
Elsewhere: RCSB PDB 5KZ6 · PDBe 5KZ6 · UniProt Q81WW1

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