MolNFT v1 · #20414 · protein

Human lysozyme labelled with two 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine

1RE2 · Protein (lysozyme): “Human lysozyme labelled with two 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine”. X-ray diffraction, 2 ligands (NAG, GAL), 1 pocket (best druggability 0.30). MolNFT v1 #20414 on GenesisL1: 3D structure…

PDB: 1RE2
Type: protein
Length: 130 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (lysozyme)
EC: 3.2.1.17
UniProt: P00695
Ligands: NAG, GAL
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (lysozyme) (EC 3.2.1.17)	protein	130	39% helix, 14% strand	P00695

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
GAL · beta-D-galactopyranose · sugar · 2 copies · chains A
GOL · Glycerol · additive · 2 copies · 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	57	0.30	0.75	13	NAG, GOL

Modifications

Observed in the structure: 4 disulfide, 2 covalent (disulfide, additive adduct).

Compared structures

1RE2 · Human lysozyme labelled with two 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine · 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 P00695
Elsewhere: RCSB PDB 1RE2 · PDBe 1RE2 · UniProt P00695

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