Arsenic in PDB 2d28: Structure of the N-Terminal Domain of Xpse (Crystal Form P43212)

The structure of Structure of the N-Terminal Domain of Xpse (Crystal Form P43212), PDB code: 2d28 was solved by Y.Chen, S.-J.Shiue, C.-W.Huang, J.-L.Chang, Y.-L.Chien, N.-T.Hu, N.-L.Chan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.00 / 2.00
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	55.914, 55.914, 104.813, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 25.2

The binding sites of Arsenic atom in the Structure of the N-Terminal Domain of Xpse (Crystal Form P43212) (pdb code 2d28). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Structure of the N-Terminal Domain of Xpse (Crystal Form P43212), PDB code: 2d28:

Arsenic binding site 1 out of 1 in the Structure of the N-Terminal Domain of Xpse (Crystal Form P43212)


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Structure of the N-Terminal Domain of Xpse (Crystal Form P43212) within 5.0Å range: probe atom residue distance (Å) B Occ C:As200 b:36.9 occ:1.00 AS C:CAC200 0.0 36.9 1.0 O2 C:CAC200 1.8 45.4 1.0 O1 C:CAC200 1.8 42.5 1.0 C2 C:CAC200 2.0 42.4 1.0 C1 C:CAC200 2.0 41.9 1.0 N C:GLY100 3.8 21.3 1.0 CA C:GLY100 4.0 22.7 1.0 C C:GLY100 4.3 22.2 1.0 CG2 C:VAL83 4.3 36.8 1.0 C C:VAL99 4.4 21.5 1.0 O C:HOH251 4.5 35.2 1.0 CG C:PRO77 4.5 49.8 1.0 CB C:PRO98 4.5 17.7 1.0 O C:GLY100 4.5 18.4 1.0 CD1 C:LEU106 4.6 16.2 1.0 O C:PRO98 4.6 17.4 1.0 C C:PRO98 4.6 16.9 1.0 N C:MSE79 4.7 66.0 1.0 CB C:MSE79 4.7 69.5 1.0 N C:VAL99 4.7 16.5 1.0 N C:GLU101 4.8 23.2 1.0 O C:HOH352 4.8 37.2 1.0 O C:GLU82 4.9 42.6 1.0 CA C:VAL99 4.9 18.8 1.0 CD C:PRO77 5.0 48.6 1.0

Y.Chen, S.-J.Shiue, C.-W.Huang, J.-L.Chang, Y.-L.Chien, N.-T.Hu, N.-L.Chan. Structure and Function of the Xpse N-Terminal Domain, An Essential Component of the Xanthomonas Campestris Type II Secretion System J.Biol.Chem. V. 280 42356 2005.
ISSN: ISSN 0021-9258
PubMed: 16162504
DOI: 10.1074/JBC.M506843200