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Magnesium in PDB 6ntd: Crystal Structure of G12V Hras-Gppnhp Bound in Complex with the Engineered Rbd Variant 12 of Craf Kinase Protein

Enzymatic activity of Crystal Structure of G12V Hras-Gppnhp Bound in Complex with the Engineered Rbd Variant 12 of Craf Kinase Protein

All present enzymatic activity of Crystal Structure of G12V Hras-Gppnhp Bound in Complex with the Engineered Rbd Variant 12 of Craf Kinase Protein:
2.7.11.1;

Protein crystallography data

The structure of Crystal Structure of G12V Hras-Gppnhp Bound in Complex with the Engineered Rbd Variant 12 of Craf Kinase Protein, PDB code: 6ntd was solved by P.Maisonneuve, I.Kurinov, S.Wiechmann, A.Ernst, F.Sicheri, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 79.47 / 3.15
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 91.761, 91.761, 151.590, 90.00, 90.00, 120.00
R / Rfree (%) 27.3 / 28.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of G12V Hras-Gppnhp Bound in Complex with the Engineered Rbd Variant 12 of Craf Kinase Protein (pdb code 6ntd). 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 Crystal Structure of G12V Hras-Gppnhp Bound in Complex with the Engineered Rbd Variant 12 of Craf Kinase Protein, PDB code: 6ntd:

Magnesium binding site 1 out of 1 in 6ntd

Go back to Magnesium Binding Sites List in 6ntd
Magnesium binding site 1 out of 1 in the Crystal Structure of G12V Hras-Gppnhp Bound in Complex with the Engineered Rbd Variant 12 of Craf Kinase Protein


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of G12V Hras-Gppnhp Bound in Complex with the Engineered Rbd Variant 12 of Craf Kinase Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg201

b:0.6
occ:1.00
 O3G A:GNP202 2.1 0.4 1.0
OG1 A:THR35 2.2 0.2 1.0
O1G A:GNP202 2.4 0.2 1.0
O1B A:GNP202 2.6 0.9 1.0
CB A:SER17 2.6 0.7 1.0
OG A:SER17 2.7 0.3 1.0
PG A:GNP202 2.7 0.8 1.0
CG2 A:THR35 2.8 0.5 1.0
CB A:THR35 3.0 0.6 1.0
OD1 A:ASP57 3.3 0.1 1.0
N A:SER17 3.4 0.6 1.0
OD2 A:ASP57 3.4 0.4 1.0
CA A:SER17 3.5 0.3 1.0
PB A:GNP202 3.7 0.2 1.0
N3B A:GNP202 3.7 0.4 1.0
CG A:ASP57 3.7 0.5 1.0
O2G A:GNP202 4.0 0.5 1.0
N A:THR35 4.0 0.1 1.0
CA A:THR35 4.1 0.4 1.0
O1A A:GNP202 4.1 0.1 1.0
O2A A:GNP202 4.2 0.8 1.0
C A:LYS16 4.4 0.8 1.0
PA A:GNP202 4.5 0.8 1.0
O A:ASP33 4.5 0.1 1.0
O3A A:GNP202 4.6 0.1 1.0
CB A:LYS16 4.7 0.0 1.0
O2B A:GNP202 4.8 0.3 1.0
C A:SER17 4.9 0.9 1.0
O A:THR35 4.9 0.5 1.0
O A:THR58 4.9 0.1 1.0
C A:THR35 5.0 0.7 1.0
CA A:LYS16 5.0 0.6 1.0

Reference:

S.Wiechmann, P.Maisonneuve, B.M.Grebbin, M.Hoffmeister, M.Kaulich, H.Clevers, K.Rajalingam, I.Kurinov, H.F.Farin, F.Sicheri, A.Ernst. Conformation-Specific Inhibitors of Activated Ras Gtpases Reveal Limited Ras Dependency of Patient-Derived Cancer Organoids. J.Biol.Chem. 2020.
ISSN: ESSN 1083-351X
PubMed: 32086379
DOI: 10.1074/JBC.RA119.011025
Page generated: Wed Aug 13 12:56:12 2025

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