MolNFT v1 · #99278 · protein

Crystal structure of glycoside hydrolase family 5 mannosidase from rhizomucor miehei, E202A mutant

4LYQ · Exo-beta-1,4-mannosidase: “Crystal structure of glycoside hydrolase family 5 mannosidase from rhizomucor miehei, E202A mutant”. X-ray diffraction, 2 ligands (BMA, MAN), 1 pocket (best druggability 0.61). MolNFT v1 #99278 on…

PDB: 4LYQ
Type: protein
Length: 414 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Exo-beta-1,4-mannosidase
EC: 3.2.1.25
Ligands: BMA, MAN
Pockets: 1 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Exo-beta-1,4-mannosidase (EC 3.2.1.25)	protein	414	42% helix, 14% strand	—

Ligands and binding sites

BMA · beta-D-mannopyranose · sugar · 2 copies · chains A
MAN · alpha-D-mannopyranose · sugar · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	158	0.61	0.83	22	MAN, BMA

Compared structures

4LYQ · Crystal Structure of Glycoside Hydrolase Family 5 Mannosidase from Rhizomucor miehei… · 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
Elsewhere: RCSB PDB 4LYQ · PDBe 4LYQ

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