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Dialyzed HEW lysozyme batch crystallized in 0.5 M YbCl3 and collected at 100 K

Analyse Dialyzed HEW lysozyme batch crystallized in 0.5 M YbCl3 and collected at 100 K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4NGW
Type: protein
Length: 129 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.37
Source: Gallus gallus
Molecule: Lysozyme C
EC: 3.2.1.17
UniProt: P00698
Ligands: YB, CL
Pockets: 1 · best druggability 0.30

Structure

x-ray diffraction · resolution 1.37 · 1 distinct chain · 41% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysozyme C (EC 3.2.1.17)	protein	129	41% helix, 11% strand	P00698

Ligands and binding sites

YB · Ytterbium (III) ion · metal · 3 copies · chains A
CL · Chloride ion · ion · 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	74	0.30	0.74	21	empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

4NGW · Dialyzed hew lysozyme batch crystallized in 0.5 M YBCL3 and collected at 100 K · 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 P00698
Elsewhere: RCSB PDB 4NGW · PDBe 4NGW · UniProt P00698

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