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Crystal structure of the eimeria tenella surface antigen protein SAG19

Analyse Crystal structure of the eimeria tenella surface antigen protein SAG19 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ZZB
Type: protein
Length: 189 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sag family member (SAG19)
UniProt: Q70CD0
Ligands: SO4
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sag family member (SAG19)	protein	189	37% helix, 14% strand	Q70CD0

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · 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	59	0.33	0.77	14	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

6ZZB · Crystal structure of the Eimeria tenella surface antigen protein SAG19 · 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 Q70CD0
Elsewhere: RCSB PDB 6ZZB · PDBe 6ZZB · UniProt Q70CD0

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