Arsenic in PDB 6vph: TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 Modified with Cacodylate and in Complex with Amp-Pnp

All present enzymatic activity of TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 Modified with Cacodylate and in Complex with Amp-Pnp:
2.7.11.1;

The structure of TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 Modified with Cacodylate and in Complex with Amp-Pnp, PDB code: 6vph was solved by D.C.Lim, M.B.Yaffe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.54 / 2.14
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	89.081, 89.081, 183.806, 90.00, 90.00, 120.00
R / Rfree (%)	18.7 / 21.7

The structure of TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 Modified with Cacodylate and in Complex with Amp-Pnp also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Arsenic atom in the TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 Modified with Cacodylate and in Complex with Amp-Pnp (pdb code 6vph). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 Modified with Cacodylate and in Complex with Amp-Pnp, PDB code: 6vph:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in the TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 Modified with Cacodylate and in Complex with Amp-Pnp


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 Modified with Cacodylate and in Complex with Amp-Pnp within 5.0Å range: probe atom residue distance (Å) B Occ A:As247 b:58.9 occ:1.00 AS A:CAS247 0.0 58.9 1.0 CE2 A:CAS247 2.0 63.1 1.0 CE1 A:CAS247 2.0 56.5 1.0 SG A:CAS247 2.2 58.0 1.0 CB A:CAS247 3.3 49.7 1.0 CG A:ARG255 4.0 62.6 1.0 CA A:CAS247 4.7 49.1 1.0 CD1 A:ILE193 4.7 29.9 1.0 CG2 A:VAL252 4.8 62.0 1.0 CB A:VAL252 4.8 68.2 1.0 CD A:ARG255 4.8 74.3 1.0 CD2 A:LEU244 4.9 34.9 1.0 CD1 A:LEU188 4.9 29.4 1.0 CG1 A:VAL252 5.0 74.4 1.0

Arsenic binding site 2 out of 2 in the TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 Modified with Cacodylate and in Complex with Amp-Pnp


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 Modified with Cacodylate and in Complex with Amp-Pnp within 5.0Å range: probe atom residue distance (Å) B Occ A:As290 b:60.7 occ:1.00 AS A:CAS290 0.0 60.7 1.0 CE1 A:CAS290 2.0 48.6 1.0 CE2 A:CAS290 2.0 49.4 1.0 SG A:CAS290 2.2 53.2 1.0 CB A:CAS290 3.2 49.6 1.0 O A:LEU289 3.5 55.8 1.0 CA A:CAS290 3.7 39.3 1.0 C A:LEU289 4.1 50.8 1.0 N A:CAS290 4.2 39.8 1.0 O A:HOH762 4.9 28.3 1.0 O A:GLY173 4.9 36.4 1.0 CD1 A:LEU293 4.9 34.5 1.0 OE1 A:GLN177 4.9 38.0 1.0

D.C.Lim, V.Joukov, T.J.Rettenmaier, A.Kumagai, W.G.Dunphy, J.A.Wells, M.B.Yaffe. Redox Priming Promotes Aurora A Activation During Mitosis. Sci.Signal. V. 13 2020.
ISSN: ESSN 1937-9145
PubMed: 32694171
DOI: 10.1126/SCISIGNAL.ABB6707