MolNFT v1 · #32617 · protein

The structure of a modular endo-beta-1,4-mannanase from cellulomonas fimi explains the product specificity of glycoside hydrolase family 26 mannanases.

2BVT: “The structure of a modular endo-beta-1,4-mannanase from cellulomonas fimi explains the product specificity of…”. X-ray diffraction, 1 ligand (BMA), 9 pockets (best druggability 0.51). MolNFT v1 #32617 on GenesisL1: 3D structure…

PDB: 2BVT
Type: protein
Length: 902 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-1,4-mannanase
EC: 3.2.1.78
UniProt: Q9XCV5
Ligands: BMA
Pockets: 9 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Beta-1,4-mannanase (EC 3.2.1.78)	protein	451	29% helix, 24% strand	Q9XCV5

Ligands and binding sites

BMA · beta-D-mannopyranose · sugar · 6 copies · chains A, B
CAC · Cacodylate ion · additive · 2 copies · chains A, B

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

Pockets

9 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	133	0.51	0.80	20	empty
2	140	0.51	0.80	21	empty
3	82	0.42	0.80	24	empty
4	76	0.42	0.80	23	empty
5	56	0.39	0.80	18	empty

Compared structures

2BVT · The structure of a modular endo-beta-1,4-mannanase from Cellulomonas fimi explains the… · 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 Q9XCV5
Elsewhere: RCSB PDB 2BVT · PDBe 2BVT · UniProt Q9XCV5

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