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T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--apo structure

Analyse T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--apo structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GUI
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: TAM, CO3, SO4
Pockets: 1 · best druggability 0.45

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysozyme (EC 3.2.1.17)	protein	162	65% helix, 9% strand	P00720

Ligands and binding sites

TAM · Tris(hydroxyethyl)aminomethane · ligand · chains A
CO3 · Carbonate ion · ion · chains A
SO4 · Sulfate ion · ion · chains A
BME · Beta-mercaptoethanol · additive · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	166	0.45	0.75	25	empty

Modifications

Observed in the structure: 2 modified, 1 disulfide (artifact, disulfide).

Compared structures

3GUI · T4 lysozyme M102E/L99A mutant with buried charge in apolar cavity--Apo structure · 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 3GUI · PDBe 3GUI · UniProt P00720

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