Research workbench

Turkey lysozyme complex with (GLCNAC)3

Analyse Turkey lysozyme complex with (GLCNAC)3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JEF
Type: protein
Length: 129 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysozyme
EC: 3.2.1.17
UniProt: P00703
Ligands: NAG, SO4
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysozyme (EC 3.2.1.17)	protein	129	41% helix, 11% strand	P00703

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
SO4 · Sulfate ion · ion · 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	58	0.32	0.76	12	NAG

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1JEF · Turkey lysozyme complex with (GLCNAC)3 · the same entry in another collection · chain A against A, TM-score 1.00
P00703 · AlphaFold monomer V2.0 prediction for lysozyme C (P00703) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P00703
Elsewhere: RCSB PDB 1JEF · PDBe 1JEF · UniProt P00703

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