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Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid substitutions at thr 59

Analyse Dissection of helix capping in T4 lysozyme by structural and thermodynamic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LYI
Type: protein
Length: 162 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: T4 lysozyme
UniProt: P00720
Ligands: CL
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 65% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	T4 lysozyme	protein	162	65% helix, 9% strand	P00720

Ligands and binding sites

CL · Chloride ion · ion · 2 copies · chains A
BME · Beta-mercaptoethanol · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	245	0.51	0.75	32	empty

Compared structures

1LYI · Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of… · 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 1LYI · PDBe 1LYI · UniProt P00720

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