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Replacements of PRO86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability

Analyse Replacements of PRO86 in phage T4 lysozyme extend an alpha-helix but do not… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1L29
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 · 67% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	T4 lysozyme (EC 3.2.1.17)	protein	164	67% 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	274	0.54	0.76	33	empty

Compared structures

1L29 · Replacements of PRO86 in phage T4 lysozyme extend an alpha-helix but do not alter protein… · 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 1L29 · PDBe 1L29 · UniProt P00720

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