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The structure and characterization of a modular endo-beta-1,4-mannanase from cellulomonas fimi

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PDB: 2BVY
Type: protein
Length: 451 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-1,4-mannanase
EC: 3.2.1.78
UniProt: Q9XCV5
Pockets: 5 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-1,4-mannanase (EC 3.2.1.78)	protein	451	28% helix, 23% strand	Q9XCV5

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A
CAC · Cacodylate ion · additive · chains A
ACT · Acetate ion · additive · chains A

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

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	152	0.49	0.78	22	empty
2	63	0.42	0.82	22	empty
3	140	0.42	0.75	29	CAC, GOL
4	54	0.31	0.76	13	empty
5	61	0.26	0.73	19	empty

Compared structures

2BVY · The structure and characterization of a modular endo-beta-1,4-mannanase from Cellulomonas… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9XCV5
Elsewhere: RCSB PDB 2BVY · PDBe 2BVY · UniProt Q9XCV5

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