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A widespread family of bacterial cell wall assembly proteins

Analyse A widespread family of bacterial cell wall assembly proteins in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2XXP
Type: protein
Length: 374 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.692
Source: STREPTOCOCCUS PNEUMONIAE
Molecule: CPS2A
UniProt: Q9ZII9
Ligands: DSL
Pockets: 4 · best druggability 0.87

Structure

x-ray diffraction · resolution 1.692 · 1 distinct chain · 39% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CPS2A	protein	374	39% helix, 27% strand	Q9ZII9

Ligands and binding sites

DSL · Mono-trans, octa-cis decaprenyl-phosphate · ligand · chains A
PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	808	0.87	0.89	60	DSL
2	157	0.50	0.79	21	PEG
3	51	0.49	0.86	17	empty
4	82	0.37	0.76	14	empty

Compared structures

2XXP · A widespread family of bacterial cell wall assembly proteins · 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 Q9ZII9
Elsewhere: RCSB PDB 2XXP · PDBe 2XXP · UniProt Q9ZII9

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