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Chitinase CHIA74 from bacillus thuringiensis

Analyse Chitinase CHIA74 from bacillus thuringiensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6BT9
Type: protein
Length: 1,251 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chitinase
UniProt: A0A243G6Q6
Ligands: CA
Pockets: 11 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chitinase	protein	625	24% helix, 33% strand	A0A243G6Q6
B	Chitinase	protein	626	23% helix, 32% strand	A0A243G6Q6

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A, B

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

Pockets

11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1112	0.76	0.78	92	empty
2	897	0.75	0.78	65	empty
3	899	0.75	0.78	67	empty
4	313	0.61	0.79	51	empty
5	128	0.49	0.79	29	empty

Interfaces

1 interface between chains.

A–B · 859 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 disulfide (disulfide).

Compared structures

6BT9 · Chitinase ChiA74 from Bacillus thuringiensis · 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 A0A243G6Q6
Elsewhere: RCSB PDB 6BT9 · PDBe 6BT9 · UniProt A0A243G6Q6

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