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Magnesium in PDB 6vpi: TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 C247V + D256N + C319V Triple Mutant Disulfide Homodimer in Complex with Amp-Pnp

Enzymatic activity of TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 C247V + D256N + C319V Triple Mutant Disulfide Homodimer in Complex with Amp-Pnp

All present enzymatic activity of TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 C247V + D256N + C319V Triple Mutant Disulfide Homodimer in Complex with Amp-Pnp:
2.7.11.1;

Protein crystallography data

The structure of TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 C247V + D256N + C319V Triple Mutant Disulfide Homodimer in Complex with Amp-Pnp, PDB code: 6vpi 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) 23.26 / 2.00
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 85.292, 85.292, 128.246, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 21.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 C247V + D256N + C319V Triple Mutant Disulfide Homodimer in Complex with Amp-Pnp (pdb code 6vpi). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 C247V + D256N + C319V Triple Mutant Disulfide Homodimer in Complex with Amp-Pnp, PDB code: 6vpi:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 6vpi

Go back to Magnesium Binding Sites List in 6vpi
Magnesium binding site 1 out of 2 in the TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 C247V + D256N + C319V Triple Mutant Disulfide Homodimer in Complex with Amp-Pnp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 C247V + D256N + C319V Triple Mutant Disulfide Homodimer in Complex with Amp-Pnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg602

b:67.5
occ:1.00
 OD1 A:ASN261 2.3 33.5 1.0
O3G A:ANP601 2.5 0.3 1.0
OD2 A:ASP274 2.6 47.7 1.0
O A:HOH889 2.6 62.8 1.0
O A:HOH785 2.7 70.4 1.0
O2A A:ANP601 2.7 96.5 1.0
N3B A:ANP601 2.9 0.5 1.0
PG A:ANP601 3.3 0.4 1.0
CG A:ASN261 3.3 30.8 1.0
CG A:ASP274 3.7 43.4 1.0
ND2 A:ASN261 3.7 25.0 1.0
MG A:MG603 3.9 77.0 1.0
PA A:ANP601 4.2 95.3 1.0
CB A:ASP274 4.2 32.6 1.0
O2G A:ANP601 4.3 0.9 1.0
PB A:ANP601 4.3 0.2 1.0
O1G A:ANP601 4.4 0.4 1.0
CB A:ASN261 4.7 29.1 1.0
OD1 A:ASP274 4.7 48.0 1.0
O3A A:ANP601 4.7 0.5 1.0
CB A:GLU260 4.8 37.5 1.0
CE A:LYS258 4.8 46.2 1.0
O2B A:ANP601 4.9 0.2 1.0
O A:GLU260 4.9 32.0 1.0
O1A A:ANP601 4.9 94.5 1.0
C A:GLU260 5.0 32.9 1.0
CA A:ASN261 5.0 31.2 1.0

Magnesium binding site 2 out of 2 in 6vpi

Go back to Magnesium Binding Sites List in 6vpi
Magnesium binding site 2 out of 2 in the TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 C247V + D256N + C319V Triple Mutant Disulfide Homodimer in Complex with Amp-Pnp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of TPX2 Residues 7-20 Fused to Aurora A Residues 116-389 C247V + D256N + C319V Triple Mutant Disulfide Homodimer in Complex with Amp-Pnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg603

b:77.0
occ:1.00
 O A:HOH882 2.6 75.0 1.0
O A:HOH889 2.8 62.8 1.0
OD2 A:ASP274 3.0 47.7 1.0
N3B A:ANP601 3.4 0.5 1.0
ND2 A:ASN256 3.5 35.9 1.0
O A:HOH743 3.6 55.9 1.0
MG A:MG602 3.9 67.5 1.0
CG A:ASP274 3.9 43.4 1.0
O A:HOH875 3.9 71.8 1.0
OD1 A:ASP274 4.0 48.0 1.0
O2G A:ANP601 4.3 0.9 1.0
O2B A:ANP601 4.4 0.2 1.0
PG A:ANP601 4.4 0.4 1.0
PB A:ANP601 4.5 0.2 1.0
O A:HOH816 4.7 67.1 1.0
CG A:ASN256 4.8 36.2 1.0
NE1 A:TRP277 4.8 50.7 1.0
O3G A:ANP601 4.8 0.3 1.0
O A:HOH711 4.9 69.7 1.0
ND2 A:ASN261 5.0 25.0 1.0

Reference:

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
Page generated: Wed Aug 13 19:17:15 2025

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