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Structure of the hyperthermostable endo-1,4-beta-D-mannanase from thermotoga petrophila rku-1 with three glycerol molecules

Analyse Structure of the hyperthermostable endo-1,4-beta-D-mannanase from thermotoga… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3PZM
Type: protein
Length: 357 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mannan endo-1,4-beta-mannosidase. glycosyl hydrolase family 5
EC: 3.2.1.78
UniProt: A5IMX7
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mannan endo-1,4-beta-mannosidase. glycosyl hydrolase family 5 (EC 3.2.1.78)	protein	357	41% helix, 17% strand	A5IMX7

Ligands and binding sites

GOL · Glycerol · additive · 3 copies · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	176	0.50	0.77	29	GOL, TRS

Compared structures

3PZM · Structure of the hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila… · 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 A5IMX7
Elsewhere: RCSB PDB 3PZM · PDBe 3PZM · UniProt A5IMX7

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