Chlorine 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:

Arsenic

(As)

2 atoms

The binding sites of Chlorine 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 Chlorine atom.
In total 2 binding sites of Chlorine 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 Chlorine binding site number: 1; 2;

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl601 b:42.9 occ:1.00 O A:HOH831 3.4 58.0 1.0 N A:GLN335 3.4 36.5 1.0 CB A:TYR334 3.7 36.3 1.0 N A:TYR334 3.8 33.2 1.0 CB A:GLN335 3.9 49.6 1.0 CB A:THR333 4.0 40.7 1.0 CA A:TYR334 4.1 36.3 1.0 CA A:GLN335 4.3 41.6 1.0 OG1 A:THR333 4.3 46.8 1.0 C A:TYR334 4.3 31.4 1.0 CD1 A:TYR334 4.3 35.5 1.0 CG A:TYR334 4.5 34.4 1.0 OE1 A:GLN335 4.5 62.6 1.0 C A:THR333 4.6 38.8 1.0 CA A:THR333 4.9 40.7 1.0 CG A:GLN335 4.9 60.6 1.0 CG2 A:THR333 5.0 43.1 1.0

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl602 b:59.0 occ:1.00 N A:HIS366 3.1 47.4 1.0 CA A:LYS365 3.7 49.9 1.0 CB A:HIS366 3.9 48.9 1.0 C A:LYS365 3.9 49.9 1.0 CA A:HIS366 4.1 47.4 1.0 CG A:LYS365 4.1 55.7 1.0 O A:LEU364 4.2 46.7 1.0 CB A:LYS365 4.4 47.4 1.0 CG2 A:VAL344 4.6 38.0 1.0 CB A:VAL344 4.7 38.8 1.0 N A:LYS365 4.8 45.7 1.0 NZ A:LYS365 4.8 62.1 1.0 CG1 A:VAL344 4.9 41.1 1.0 C A:LEU364 4.9 45.0 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