Research workbench

Lysozyme complex with 4-methyl-umbelliferyl chitotriose

Analyse Lysozyme complex with 4-methyl-umbelliferyl chitotriose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BB6
Type: protein
Length: 129 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysozyme
EC: 3.2.1.17
UniProt: P11941
Ligands: UMG
Pockets: 1 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysozyme (EC 3.2.1.17)	protein	129	38% helix, 11% strand	P11941

Ligands and binding sites

UMG · Methyl-umbellifertl-N-acetyl-chitotriose · ligand · 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	89	0.38	0.76	15	UMG

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1BB6 · Lysozyme complex with 4-methyl-umbelliferyl chitotriose · the same entry in another collection · chain A against A, TM-score 1.00
P11941 · AlphaFold monomer V2.0 prediction for lysozyme C II (P11941) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P11941
Elsewhere: RCSB PDB 1BB6 · PDBe 1BB6 · UniProt P11941

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