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Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability

Analyse Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LWG
Type: protein
Length: 162 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysozyme
EC: 3.2.1.17
UniProt: P00720
Ligands: K, CL, PO4
Pockets: 2 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 67% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysozyme (EC 3.2.1.17)	protein	162	67% helix, 9% strand	P00720

Ligands and binding sites

K · Potassium ion · metal · chains A
CL · Chloride ion · ion · 3 copies · chains A
PO4 · Phosphate ion · ion · chains A
HED · 2-hydroxyethyl disulfide · additive · 3 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	300	0.55	0.75	30	empty
2	56	0.40	0.81	13	HED

Compared structures

1LWG · Multiple Methionine Substitutions are Tolerated in T4 Lysozyme and have Coupled Effects… · 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 1LWG · PDBe 1LWG · UniProt P00720

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