MolNFT v1 · #34299 · protein

Crystal structure of chitinase C from streptomyces griseus HUT6037

2DBT: “Crystal structure of chitinase C from streptomyces griseus HUT6037”. X-ray diffraction, 4 pockets (best druggability 0.63). MolNFT v1 #34299 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2DBT
Type: protein
Length: 615 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chitinase C
EC: 3.2.1.14
UniProt: O50152
Pockets: 4 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Chitinase C (EC 3.2.1.14)	protein	205	51% helix, 1% strand	O50152

Ligands and binding sites

EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 3 copies · chains A, C, B

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

Pockets

4 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	308	0.63	0.80	33	EPE
2	282	0.61	0.79	30	EPE
3	170	0.46	0.75	24	EPE
4	63	0.39	0.80	12	empty

Interfaces

2 interfaces between chains.

A–C · 758 Å² buried · 3 hydrogen bonds · protein-protein
B–C · 687 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

2DBT · Crystal structure of chitinase C from Streptomyces griseus HUT6037 · 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 O50152
Elsewhere: RCSB PDB 2DBT · PDBe 2DBT · UniProt O50152

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