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T4 Lysozyme mutant L99A at 100 MPa

Analyse T4 Lysozyme mutant L99A at 100 MPa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2B73
Type: protein
Length: 162 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.15
Source: Enterobacteria phage T4
Molecule: Lysozyme
EC: 3.2.1.17
UniProt: P00720
Ligands: CL
Pockets: 1 · best druggability 0.52

Structure

x-ray diffraction · resolution 2.15 · 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

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	247	0.52	0.75	30	empty

Compared structures

2B73 · T4 lysozyme mutant L99A at 100 mpa · 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 2B73 · PDBe 2B73 · UniProt P00720

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