MolNFT v1 · #20431 · protein

Human lysozyme with man-B1,4-glcnac covalently attached to ASP53

1REM: “Human lysozyme with man-B1,4-glcnac covalently attached to ASP53”. X-ray diffraction, 3 ligands (NAG, BMA, NO3), 1 pocket (best druggability 0.37). MolNFT v1 #20431 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1REM
Type: protein
Length: 130 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysozyme
EC: 3.2.1.17
UniProt: P00695
Ligands: NAG, BMA, NO3
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysozyme (EC 3.2.1.17)	protein	130	38% helix, 14% strand	P00695

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
BMA · beta-D-mannopyranose · sugar · chains A
NO3 · Nitrate ion · ion · chains A
PGR · R-1,2-propanediol · 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	67	0.37	0.78	16	NAG, PGR

Modifications

Observed in the structure: 4 disulfide, 1 covalent (disulfide, additive adduct).

Compared structures

1REM · Human lysozyme with man-B1,4-glcnac covalently attached to ASP53 · 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 1REM · PDBe 1REM · UniProt P00695

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.