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The crystal structure of a complex between bulgecin, a bacterial metabolite, and lysozyme from the rainbow trout

Analyse The crystal structure of a complex between bulgecin, a bacterial metabolite… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LMC
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: BUL
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysozyme (EC 3.2.1.17)	protein	129	39% helix, 11% strand	P11941

Ligands and binding sites

BUL · Bulgecin A · 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	57	0.31	0.76	12	BUL

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1LMC · The crystal structure of a complex between bulgecin, a bacterial metabolite, and lysozyme… · 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 1LMC · PDBe 1LMC · UniProt P11941

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