Magnesium in PDB 6e6h: Nras G13D Bound to Gppnhp (N13GNP)

Protein crystallography data

The structure of Nras G13D Bound to Gppnhp (N13GNP), PDB code: 6e6h was solved by C.W.Johnson, C.Mattos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.50 / 1.99
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 59.553, 39.565, 65.016, 90.00, 106.40, 90.00
R / Rfree (%) 17.9 / 23.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Nras G13D Bound to Gppnhp (N13GNP) (pdb code 6e6h). 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 Nras G13D Bound to Gppnhp (N13GNP), PDB code: 6e6h:

Magnesium binding site 1 out of 1 in 6e6h

Go back to Magnesium Binding Sites List in 6e6h
Magnesium binding site 1 out of 1 in the Nras G13D Bound to Gppnhp (N13GNP)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Nras G13D Bound to Gppnhp (N13GNP) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg201

b:24.7
occ:1.00
O1G A:GNP202 1.9 29.7 1.0
O1B A:GNP202 2.0 21.1 1.0
O A:HOH317 2.0 22.3 1.0
O A:HOH339 2.1 27.5 1.0
OG A:SER17 2.2 21.3 1.0
O A:HOH310 2.3 23.3 1.0
CB A:SER17 3.0 17.0 1.0
PG A:GNP202 3.2 33.7 1.0
PB A:GNP202 3.2 29.4 1.0
N3B A:GNP202 3.4 22.6 1.0
N A:SER17 3.7 19.6 1.0
CA A:SER17 3.9 16.8 1.0
O2A A:GNP202 4.0 26.6 1.0
OD2 A:ASP57 4.0 27.9 1.0
O3G A:GNP202 4.1 32.1 1.0
OD1 A:ASP57 4.1 24.0 1.0
O2B A:GNP202 4.1 26.9 1.0
O3A A:GNP202 4.3 17.1 1.0
O2G A:GNP202 4.3 35.5 1.0
CG A:ASP57 4.5 35.0 1.0
PA A:GNP202 4.5 23.7 1.0
CB A:THR35 4.5 33.5 1.0
OG1 A:THR35 4.6 31.2 1.0
O1A A:GNP202 4.6 20.4 1.0
O A:THR58 4.7 29.7 1.0
O A:THR35 4.7 32.2 1.0
CB A:LYS16 4.8 18.0 1.0
CE A:LYS16 4.8 22.3 1.0
C A:LYS16 4.8 21.6 1.0
NZ A:LYS16 5.0 20.1 1.0

Reference:

C.W.Johnson, Y.J.Lin, D.Reid, J.Parker, S.Pavlopoulos, P.Dischinger, C.Graveel, A.J.Aguirre, M.Steensma, K.M.Haigis, C.Mattos. Isoform-Specific Destabilization of the Active Site Reveals A Molecular Mechanism of Intrinsic Activation of Kras G13D. Cell Rep V. 28 1538 2019.
ISSN: ESSN 2211-1247
PubMed: 31390567
DOI: 10.1016/J.CELREP.2019.07.026
Page generated: Mon Dec 14 22:38:01 2020

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