Zinc in PDB 8igt: Crystal Structure of Intracellular B30.2 Domain of BTN2A1

The structure of Crystal Structure of Intracellular B30.2 Domain of BTN2A1, PDB code: 8igt was solved by L.J.Yuan, Y.Y.Yang, X.Li, N.N.Cai, C.C.Chen, R.T.Guo, Y.H.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.67 / 1.56
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	73.957, 78.889, 41.682, 90, 90, 90
R / Rfree (%)	15.5 / 17.3

The binding sites of Zinc atom in the Crystal Structure of Intracellular B30.2 Domain of BTN2A1 (pdb code 8igt). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Intracellular B30.2 Domain of BTN2A1, PDB code: 8igt:

Zinc binding site 1 out of 1 in the Crystal Structure of Intracellular B30.2 Domain of BTN2A1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Intracellular B30.2 Domain of BTN2A1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:21.6 occ:1.00 NE2 A:HIS530 2.0 21.3 1.0 NE2 A:HIS357 2.1 21.6 1.0 NE2 A:HIS532 2.1 22.4 1.0 SG A:CYS353 2.4 13.3 0.5 SG A:CYS353 2.5 14.3 0.5 CE1 A:HIS357 2.8 28.4 1.0 CE1 A:HIS530 2.9 27.8 1.0 CD2 A:HIS530 3.0 22.6 1.0 CD2 A:HIS532 3.0 22.7 1.0 CE1 A:HIS532 3.1 22.6 1.0 CB A:CYS353 3.2 15.1 0.5 CD2 A:HIS357 3.2 25.7 1.0 CB A:CYS353 3.3 14.7 0.5 ND1 A:HIS357 4.0 30.6 1.0 ND1 A:HIS530 4.0 26.3 1.0 CG A:HIS530 4.1 22.0 1.0 CG A:HIS532 4.2 20.9 1.0 ND1 A:HIS532 4.2 21.7 1.0 O A:HOH712 4.2 32.5 1.0 CG A:HIS357 4.2 24.1 1.0 O A:PHE355 4.5 17.1 1.0 CG A:PHE342 4.5 17.9 1.0 CB A:PHE342 4.6 15.3 1.0 CA A:CYS353 4.6 13.8 0.5 CA A:CYS353 4.7 13.9 0.5 CD1 A:PHE342 4.7 19.8 1.0 CD2 A:PHE342 4.9 23.5 1.0

Y.Y.Yang, P.P.Shen, X.Li, S.M.Yi, M.T.Zhang, J.-W.Huang, C.-C.Chen, R.-T.Guo. Phosphoantigens Glue Butyrophilin 3A1 and 2A1 to Activate VGAMMA9VDELTA2 T Cells. Nature 2023.
ISSN: ESSN 1476-4687
DOI: 10.1038/S41586-023-06525-3