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The response of T4 lysozyme to large-to-small substitutions within the core and its relation to the hydrophobic effect

Analyse The response of T4 lysozyme to large-to-small substitutions within the core and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 241L
Type: protein
Length: 162 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.7
Source: Enterobacteria phage T4
Molecule: T4 lysozyme
EC: 3.2.1.17
UniProt: P00720
Ligands: CL
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · resolution 1.7 · 1 distinct chain · 66% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	T4 lysozyme (EC 3.2.1.17)	protein	162	66% helix, 9% strand	P00720

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A
HED · 2-hydroxyethyl disulfide · 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	231	0.50	0.75	25	empty

Compared structures

241L · The response of T4 lysozyme to large-to-small substitutions within the core and its… · 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 P00720
Elsewhere: RCSB PDB 241L · PDBe 241L · UniProt P00720

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