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3D-structure of the modular autolysin lytc from streptococcus pneumoniae at 1.6 a resolution

Analyse 3D-structure of the modular autolysin lytc from streptococcus pneumoniae at 1.6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WW5
Type: protein
Length: 431 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 1,4-beta-N-acetylmuramidase
EC: 3.2.1.17
UniProt: Q9Z4J8
Ligands: CHT, CL
Pockets: 3 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	1,4-beta-N-acetylmuramidase (EC 3.2.1.17)	protein	431	17% helix, 38% strand	Q9Z4J8

Ligands and binding sites

CHT · Choline ion · ligand · 7 copies · chains A
CL · Chloride ion · ion · 2 copies · chains A
GOL · Glycerol · additive · 7 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	187	0.47	0.75	28	empty
2	71	0.41	0.79	18	empty
3	110	0.39	0.76	19	empty

Compared structures

2WW5 · 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A… · 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 Q9Z4J8
Elsewhere: RCSB PDB 2WW5 · PDBe 2WW5 · UniProt Q9Z4J8

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