MolNFT v1 · #13129 · protein

Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding

1L23 · T4 lysozyme: “Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding”. X-ray diffraction, 1 pocket (best druggability 0.54). MolNFT v1 #13129 on GenesisL1: 3D structure, binding sites…

PDB: 1L23
Type: protein
Length: 164 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: T4 lysozyme
EC: 3.2.1.17
UniProt: P00720
Pockets: 1 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 64% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	T4 lysozyme (EC 3.2.1.17)	protein	164	64% helix, 9% strand	P00720

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	263	0.54	0.76	30	empty

Compared structures

1L23 · Enhanced protein thermostability from site-directed mutations that decrease the entropy… · 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 1L23 · PDBe 1L23 · UniProt P00720

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