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Magnesium in PDB 2qoc: Human EPHA3 Kinase Domain, Phosphorylated, Amp-Pnp Bound Structure

Enzymatic activity of Human EPHA3 Kinase Domain, Phosphorylated, Amp-Pnp Bound Structure

All present enzymatic activity of Human EPHA3 Kinase Domain, Phosphorylated, Amp-Pnp Bound Structure:
2.7.10.1;

Protein crystallography data

The structure of Human EPHA3 Kinase Domain, Phosphorylated, Amp-Pnp Bound Structure, PDB code: 2qoc was solved by T.Davis, J.R.Walker, E.M.Newman, F.Mackenzie, C.Butler-Cole, J.Weigelt, M.Sundstrom, C.H.Arrowsmith, A.M.Edwards, A.Bochkarev, S.Dhe-Paganon, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.45 / 1.25
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 53.790, 38.337, 76.439, 90.00, 102.07, 90.00
R / Rfree (%) 16.9 / 18.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Human EPHA3 Kinase Domain, Phosphorylated, Amp-Pnp Bound Structure (pdb code 2qoc). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Human EPHA3 Kinase Domain, Phosphorylated, Amp-Pnp Bound Structure, PDB code: 2qoc:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2qoc

Go back to Magnesium Binding Sites List in 2qoc
Magnesium binding site 1 out of 2 in the Human EPHA3 Kinase Domain, Phosphorylated, Amp-Pnp Bound Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human EPHA3 Kinase Domain, Phosphorylated, Amp-Pnp Bound Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1

b:15.2
occ:0.50
O3G A:ANP949 1.1 15.6 0.4
O1A A:ANP949 1.7 14.9 0.6
O A:HOH1372 1.7 34.7 1.0
PA A:ANP949 2.5 14.1 0.6
PG A:ANP949 2.6 9.1 0.4
O3G A:ANP949 2.7 12.1 0.6
O2A A:ANP949 2.7 12.1 0.6
O A:HOH1368 3.2 19.6 1.0
O1B A:ANP949 3.3 11.6 0.5
O2G A:ANP949 3.4 14.0 0.4
O1G A:ANP949 3.6 15.0 0.4
N3B A:ANP949 3.7 9.4 0.5
O5' A:ANP949 3.7 15.3 1.0
O3A A:ANP949 3.7 13.4 0.6
CA A:GLY630 3.9 26.8 1.0
PG A:ANP949 4.1 10.9 0.6
PB A:ANP949 4.2 10.9 0.5
MG A:MG2 4.2 25.9 1.0
O A:ALA629 4.2 26.5 1.0
C5' A:ANP949 4.3 14.9 1.0
N A:GLU631 4.7 27.0 1.0
N3B A:ANP949 4.8 12.6 0.5
O A:HOH1340 4.8 3.5 0.5
O1G A:ANP949 4.8 10.9 0.6
C A:GLY630 4.8 27.0 1.0
N A:GLY630 4.8 26.8 1.0
O A:HOH1344 4.9 29.8 1.0
C A:ALA629 4.9 26.2 1.0

Magnesium binding site 2 out of 2 in 2qoc

Go back to Magnesium Binding Sites List in 2qoc
Magnesium binding site 2 out of 2 in the Human EPHA3 Kinase Domain, Phosphorylated, Amp-Pnp Bound Structure


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human EPHA3 Kinase Domain, Phosphorylated, Amp-Pnp Bound Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2

b:25.9
occ:1.00
O A:HOH1340 2.0 3.5 0.5
OD1 A:ASN751 2.8 10.5 1.0
O1B A:ANP949 2.8 11.6 0.5
O A:HOH1281 2.9 18.1 1.0
O A:HOH1368 3.0 19.6 1.0
OD2 A:ASP764 3.0 9.8 0.5
O1G A:ANP949 3.0 10.9 0.6
O2A A:ANP949 3.1 12.1 0.6
PG A:ANP949 3.6 10.9 0.6
O3G A:ANP949 3.6 12.1 0.6
CB A:ASP764 3.6 10.4 1.0
CG A:ASP764 3.7 9.2 0.5
O A:ARG750 3.7 7.1 0.5
N3B A:ANP949 3.7 12.6 0.5
O3A A:ANP949 3.9 13.4 0.6
O A:HOH1344 3.9 29.8 1.0
PA A:ANP949 3.9 14.1 0.6
O A:ARG750 3.9 7.7 0.5
CG A:ASN751 4.0 8.9 1.0
O A:HOH1149 4.0 32.1 1.0
O A:HOH991 4.1 13.1 1.0
PB A:ANP949 4.2 10.9 0.5
MG A:MG1 4.2 15.2 0.5
O A:HOH1369 4.2 22.3 1.0
O3G A:ANP949 4.4 15.6 0.4
CA A:ASN751 4.4 7.2 1.0
C A:ARG750 4.7 6.8 0.5
O1A A:ANP949 4.7 14.9 0.6
CB A:ASN751 4.7 6.7 1.0
C A:ARG750 4.7 7.2 0.5
OD1 A:ASP764 4.8 10.2 0.5
CA A:ASP764 4.9 9.9 1.0
ND2 A:ASN751 4.9 10.0 1.0
N A:ASN751 5.0 6.9 1.0
OG A:SER763 5.0 9.5 0.5

Reference:

T.L.Davis, J.R.Walker, P.Loppnau, C.Butler-Cole, A.Allali-Hassani, S.Dhe-Paganon. Autoregulation By the Juxtamembrane Region of the Human Ephrin Receptor Tyrosine Kinase A3 (EPHA3). Structure V. 16 873 2008.
ISSN: ISSN 0969-2126
PubMed: 18547520
DOI: 10.1016/J.STR.2008.03.008
Page generated: Wed Aug 14 02:48:54 2024

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