Research workbench

Sad structure of hen egg white lysozyme recovered by inverse beam geometry data collection and univariate analysis

Analyse Sad structure of hen egg white lysozyme recovered by inverse beam geometry data… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SIM
Type: protein
Length: 129 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysozyme C
EC: 3.2.1.17
UniProt: P00698
Ligands: NA, CL
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysozyme C (EC 3.2.1.17)	protein	129	40% helix, 11% strand	P00698

Ligands and binding sites

NA · Sodium ion · metal · chains A
CL · Chloride ion · ion · 8 copies · chains A
EDO · 1,2-ethanediol · additive · 3 copies · chains A
ACT · Acetate ion · 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	71	0.34	0.76	16	EDO

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

6SIM · SAD structure of Hen Egg White Lysozyme recovered by inverse beam geometry data… · 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 6SIM · PDBe 6SIM · UniProt P00698

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