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Comparison of radiation-induced decay and structure refinement from X- ray data collected from lysozyme crystals at low and ambient temperatures

Analyse Comparison of radiation-induced decay and structure refinement from X- ray data… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LYT
Type: protein
Length: 258 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hen egg white lysozyme
EC: 3.2.1.17
UniProt: P00698
Pockets: 2 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hen egg white lysozyme (EC 3.2.1.17)	protein	129	39% helix, 12% strand	P00698

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	66	0.35	0.77	18	empty
2	77	0.32	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 350 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

3LYT · Comparison of radiation-induced decay and structure refinement from X-ray data collected… · 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 3LYT · PDBe 3LYT · UniProt P00698

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