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Structure of the C-terminal domain of sex pheromone staph-CAM373 precursor from staphylococcus aureus

Analyse Structure of the C-terminal domain of sex pheromone staph-CAM373 precursor from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2QX2
Type: protein
Length: 318 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sex pheromone staph-CAM373
UniProt: Q99SY4
Pockets: 3 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sex pheromone staph-CAM373	protein	318	33% helix, 28% strand	Q99SY4

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 5 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	188	0.50	0.76	26	EDO
2	155	0.49	0.78	30	empty
3	155	0.41	0.74	25	empty

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

2QX2 · Structure of the C-terminal domain of sex pheromone staph-cAM373 precursor from… · 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 Q99SY4
Elsewhere: RCSB PDB 2QX2 · PDBe 2QX2 · UniProt Q99SY4

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