MolNFT v1 · #108304 · protein

High resolution structure of the full length tri-modular endo-beta-1,4-glucanase B (CEL5B) from bacillus halodurans

4V2X · Endo-beta-1,4-glucanase (cellulase B): “High resolution structure of the full length tri-modular endo-beta-1,4-glucanase B (CEL5B) from bacillus…”. X-ray diffraction, 1 ligand (CA), 3 pockets (best druggability 0.55). MolNFT v1…

PDB: 4V2X
Type: protein
Length: 534 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-beta-1,4-glucanase (cellulase B)
UniProt: Q9KF82
Ligands: CA
Pockets: 3 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-beta-1,4-glucanase (cellulase B)	protein	534	32% helix, 27% strand	Q9KF82

Ligands and binding sites

CA · Calcium ion · metal · 2 copies · chains A
GOL · Glycerol · additive · 6 copies · chains A
ACT · Acetate ion · additive · chains A
CAC · Cacodylate ion · additive · 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	293	0.55	0.76	31	CAC
2	187	0.50	0.77	29	GOL
3	56	0.25	0.72	17	empty

Compared structures

4V2X · High resolution structure of the full length tri-modular endo-beta-1, 4-glucanase B… · 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 Q9KF82
Elsewhere: RCSB PDB 4V2X · PDBe 4V2X · UniProt Q9KF82

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