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Magnesium in PDB 7scw: Kras Full Length Wild-Type in Complex with RGL1 Ras Association Domain

Enzymatic activity of Kras Full Length Wild-Type in Complex with RGL1 Ras Association Domain

All present enzymatic activity of Kras Full Length Wild-Type in Complex with RGL1 Ras Association Domain:
3.6.5.2;

Protein crystallography data

The structure of Kras Full Length Wild-Type in Complex with RGL1 Ras Association Domain, PDB code: 7scw was solved by B.J.Eves, D.A.Kuntz, M.Ikura, C.B.Marshall, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.45 / 1.98
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 91.064, 91.064, 132.896, 90, 90, 120
R / Rfree (%) 15.6 / 19.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Kras Full Length Wild-Type in Complex with RGL1 Ras Association Domain (pdb code 7scw). 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 Kras Full Length Wild-Type in Complex with RGL1 Ras Association Domain, PDB code: 7scw:

Magnesium binding site 1 out of 1 in 7scw

Go back to Magnesium Binding Sites List in 7scw
Magnesium binding site 1 out of 1 in the Kras Full Length Wild-Type in Complex with RGL1 Ras Association Domain


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Kras Full Length Wild-Type in Complex with RGL1 Ras Association Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg201

b:14.7
occ:1.00
HOG2 A:GSP202 1.3 19.8 1.0
O A:HOH352 2.0 11.9 1.0
O2B A:GSP202 2.0 12.2 1.0
OG1 A:THR35 2.1 13.8 1.0
OG A:SER17 2.1 10.5 1.0
O A:HOH331 2.1 13.7 1.0
O2G A:GSP202 2.1 16.5 1.0
HB2 A:SER17 3.0 14.6 1.0
HB A:THR35 3.0 20.3 1.0
CB A:SER17 3.1 12.1 1.0
CB A:THR35 3.1 16.9 1.0
PB A:GSP202 3.2 13.7 1.0
PG A:GSP202 3.2 24.2 1.0
H A:SER17 3.3 14.3 1.0
H A:THR35 3.4 19.8 1.0
O3B A:GSP202 3.5 14.5 1.0
HOG3 A:GSP202 3.7 32.1 1.0
HB3 A:SER17 3.8 14.6 1.0
N A:THR35 3.9 16.5 1.0
N A:SER17 3.9 11.9 1.0
O3G A:GSP202 3.9 26.8 1.0
OD2 A:ASP57 4.0 24.2 1.0
HB2 A:LYS16 4.0 15.8 1.0
HG21 A:THR35 4.0 19.1 1.0
CA A:SER17 4.1 11.7 1.0
O2A A:GSP202 4.1 14.4 1.0
CA A:THR35 4.1 16.4 1.0
HE2 A:LYS16 4.1 18.7 1.0
OD1 A:ASP57 4.2 25.6 1.0
CG2 A:THR35 4.2 15.9 1.0
O3A A:GSP202 4.3 12.8 1.0
O A:HOH333 4.3 16.6 1.0
O1B A:GSP202 4.3 12.4 1.0
O A:ASP33 4.3 21.2 1.0
HA A:PRO34 4.4 23.4 1.0
HA A:SER17 4.4 14.1 1.0
PA A:GSP202 4.5 15.7 1.0
CG A:ASP57 4.5 19.9 1.0
O A:THR58 4.5 17.6 1.0
HA A:THR35 4.6 19.7 1.0
O1A A:GSP202 4.6 13.0 1.0
HG23 A:THR35 4.7 19.1 1.0
S1G A:GSP202 4.7 27.2 1.0
C A:PRO34 4.7 18.1 1.0
HZ1 A:LYS16 4.8 22.4 1.0
HG22 A:THR35 4.9 19.1 1.0
CB A:LYS16 4.9 13.1 1.0
C A:LYS16 5.0 11.9 1.0

Reference:

B.J.Eves, T.Gebregiworgis, G.M.C.Gasmi-Seabrook, D.A.Kuntz, G.G.Prive, C.B.Marshall, M.Ikura. Structures of RGL1 Ras-Association Domain in Complex with Kras and the Oncogenic G12V Mutant. J.Mol.Biol. V. 434 67527 2022.
ISSN: ESSN 1089-8638
PubMed: 35257782
DOI: 10.1016/J.JMB.2022.167527
Page generated: Thu Oct 3 08:43:08 2024

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