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Magnesium in PDB 3fxx: Human EPHA3 Kinase and Juxtamembrane Region Bound to Substrate Kqwdnye[Ptyr]Iw

Enzymatic activity of Human EPHA3 Kinase and Juxtamembrane Region Bound to Substrate Kqwdnye[Ptyr]Iw

All present enzymatic activity of Human EPHA3 Kinase and Juxtamembrane Region Bound to Substrate Kqwdnye[Ptyr]Iw:
2.7.10.1;

Protein crystallography data

The structure of Human EPHA3 Kinase and Juxtamembrane Region Bound to Substrate Kqwdnye[Ptyr]Iw, PDB code: 3fxx was solved by T.Davis, J.R.Walker, F.Mackenzie, J.Weigelt, C.Bountra, 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) 26.47 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 53.463, 38.201, 76.649, 90.00, 102.15, 90.00
R / Rfree (%) 16.6 / 19.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Human EPHA3 Kinase and Juxtamembrane Region Bound to Substrate Kqwdnye[Ptyr]Iw (pdb code 3fxx). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Human EPHA3 Kinase and Juxtamembrane Region Bound to Substrate Kqwdnye[Ptyr]Iw, PDB code: 3fxx:

Magnesium binding site 1 out of 1 in 3fxx

Go back to Magnesium Binding Sites List in 3fxx
Magnesium binding site 1 out of 1 in the Human EPHA3 Kinase and Juxtamembrane Region Bound to Substrate Kqwdnye[Ptyr]Iw


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 and Juxtamembrane Region Bound to Substrate Kqwdnye[Ptyr]Iw within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg991

b:46.6
occ:1.00
O2B A:ANP992 1.9 33.8 0.5
O1G A:ANP992 1.9 31.6 0.5
O A:HOH301 2.0 42.1 1.0
O2A A:ANP992 2.1 40.3 1.0
O A:HOH154 2.4 32.7 1.0
O A:HOH81 2.5 43.3 1.0
PG A:ANP992 2.9 30.2 0.5
PB A:ANP992 3.0 32.4 0.5
PA A:ANP992 3.3 41.0 1.0
N3B A:ANP992 3.3 31.7 0.5
O3A A:ANP992 3.5 39.3 1.0
O2G A:ANP992 3.7 31.1 0.5
O A:HOH202 3.9 35.8 1.0
O A:ARG750 4.2 17.9 1.0
O1A A:ANP992 4.2 42.1 1.0
O1B A:ANP992 4.2 33.6 0.5
O3G A:ANP992 4.3 29.9 0.5
O5' A:ANP992 4.4 38.7 1.0
C5' A:ANP992 4.4 36.0 1.0
OD1 A:ASN751 4.6 21.5 1.0
OG A:SER706 4.7 16.2 0.5
O A:HOH45 4.7 31.7 1.0
O3' A:ANP992 4.8 37.5 1.0
OD2 A:ASP764 4.9 24.3 0.5
O A:HOH76 4.9 34.0 1.0
C3' A:ANP992 5.0 34.2 1.0

Reference:

T.L.Davis, J.R.Walker, A.Allali-Hassani, S.A.Parker, B.E.Turk, S.Dhe-Paganon. Structural Recognition of An Optimized Substrate For the Ephrin Family of Receptor Tyrosine Kinases. Febs J. V. 276 4395 2009.
ISSN: ISSN 1742-464X
PubMed: 19678838
DOI: 10.1111/J.1742-4658.2009.07147.X
Page generated: Mon Dec 14 08:09:29 2020

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