Magnesium in PDB 5uhv: Wild-Type Nras Bound to Gppnhp

Protein crystallography data

The structure of Wild-Type Nras Bound to Gppnhp, PDB code: 5uhv was solved by D.Reid, C.Johnson, S.Salter, C.Mattos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.50 / 1.67
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 39.007, 39.007, 159.175, 90.00, 90.00, 120.00
R / Rfree (%) 18.7 / 22.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Wild-Type Nras Bound to Gppnhp (pdb code 5uhv). 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 Wild-Type Nras Bound to Gppnhp, PDB code: 5uhv:

Magnesium binding site 1 out of 1 in 5uhv

Go back to Magnesium Binding Sites List in 5uhv
Magnesium binding site 1 out of 1 in the Wild-Type Nras Bound to Gppnhp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Wild-Type Nras Bound to Gppnhp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg202

b:19.9
occ:1.00
O2G A:GNP201 2.0 22.1 1.0
O2B A:GNP201 2.0 19.1 1.0
OG A:SER17 2.1 18.9 1.0
O A:HOH340 2.1 21.9 1.0
OG1 A:THR35 2.1 20.4 1.0
O A:HOH317 2.2 19.4 1.0
CB A:SER17 3.1 18.9 1.0
CB A:THR35 3.1 20.8 1.0
PG A:GNP201 3.2 22.0 1.0
PB A:GNP201 3.2 19.6 1.0
N3B A:GNP201 3.4 18.9 1.0
N A:SER17 3.8 16.8 1.0
N A:THR35 3.8 23.3 1.0
OD2 A:ASP57 3.9 23.6 1.0
CA A:SER17 4.0 20.1 1.0
CA A:THR35 4.1 23.5 1.0
O2A A:GNP201 4.1 20.3 1.0
OD1 A:ASP57 4.1 22.1 1.0
O3G A:GNP201 4.1 19.6 1.0
CG2 A:THR35 4.2 26.3 1.0
O3A A:GNP201 4.2 18.2 1.0
O A:HOH345 4.2 31.2 1.0
O1B A:GNP201 4.2 19.0 1.0
O1G A:GNP201 4.3 23.7 1.0
O A:THR58 4.4 26.5 1.0
CG A:ASP57 4.4 23.1 1.0
PA A:GNP201 4.5 19.9 1.0
O A:ASP33 4.5 24.0 1.0
O1A A:GNP201 4.7 19.8 1.0
CB A:LYS16 4.7 17.3 1.0
C A:PRO34 4.7 25.2 1.0
C A:LYS16 4.9 18.1 1.0
CE A:LYS16 4.9 19.9 1.0

Reference:

C.W.Johnson, D.Reid, J.A.Parker, S.Salter, R.Knihtila, P.Kuzmic, C.Mattos. The Small Gtpases K-Ras, N-Ras, and H-Ras Have Distinct Biochemical Properties Determined By Allosteric Effects. J. Biol. Chem. V. 292 12981 2017.
ISSN: ESSN 1083-351X
PubMed: 28630043
DOI: 10.1074/JBC.M117.778886
Page generated: Mon Dec 14 21:16:09 2020

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