MolNFT v1 · #111742 · protein

Crystal structure of a tri-modular GH5 (subfamily 4) endo-beta-1, 4- glucanase from bacillus licheniformis complexed with cellotetraose

4YZT · Cellulose hydrolase: “Crystal structure of a tri-modular GH5 (subfamily 4) endo-beta-1, 4- glucanase from bacillus licheniformis…”. X-ray diffraction, 1 ligand (BGC), 3 pockets (best druggability 0.57). MolNFT v1 #111742 on…

PDB: 4YZT
Type: protein
Length: 512 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellulose hydrolase
EC: 3.2.1.4
UniProt: D1L8C7
Ligands: BGC
Pockets: 3 · best druggability 0.57

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cellulose hydrolase (EC 3.2.1.4)	protein	512	31% helix, 27% strand	D1L8C7

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 4 copies · chains A
EDO · 1,2-ethanediol · additive · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	314	0.57	0.76	35	empty
2	126	0.37	0.73	20	BGC
3	61	0.26	0.72	13	empty

Compared structures

4YZT · Crystal structure of a tri-modular GH5 (subfamily 4) endo-beta-1, 4-glucanase from… · 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 D1L8C7
Elsewhere: RCSB PDB 4YZT · PDBe 4YZT · UniProt D1L8C7

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