MolNFT v1 · #14103 · protein

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

1LYI: “Dissection of helix capping in T4 lysozyme by structural and thermodynamic analysis of six amino acid…”. X-ray diffraction, 1 ligand (CL), 1 pocket (best druggability 0.51). MolNFT v1 #14103 on GenesisL1: 3D structure, binding sites…

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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