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Magnesium in PDB 7jhp: Crystal Structure of Hras in Complex with the Ras-Binding and Cysteine-Rich Domains of Craf-Kinase

Enzymatic activity of Crystal Structure of Hras in Complex with the Ras-Binding and Cysteine-Rich Domains of Craf-Kinase

All present enzymatic activity of Crystal Structure of Hras in Complex with the Ras-Binding and Cysteine-Rich Domains of Craf-Kinase:
2.7.11.1;

Protein crystallography data

The structure of Crystal Structure of Hras in Complex with the Ras-Binding and Cysteine-Rich Domains of Craf-Kinase, PDB code: 7jhp was solved by T.Cookis, C.Mattos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.61 / 2.77
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 94.487, 44.353, 74.395, 90.00, 103.95, 90.00
R / Rfree (%) 21.1 / 26.4

Other elements in 7jhp:

The structure of Crystal Structure of Hras in Complex with the Ras-Binding and Cysteine-Rich Domains of Craf-Kinase also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Hras in Complex with the Ras-Binding and Cysteine-Rich Domains of Craf-Kinase (pdb code 7jhp). 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 Hras in Complex with the Ras-Binding and Cysteine-Rich Domains of Craf-Kinase, PDB code: 7jhp:

Magnesium binding site 1 out of 1 in 7jhp

Go back to Magnesium Binding Sites List in 7jhp
Magnesium binding site 1 out of 1 in the Crystal Structure of Hras in Complex with the Ras-Binding and Cysteine-Rich Domains of Craf-Kinase


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 Hras in Complex with the Ras-Binding and Cysteine-Rich Domains of Craf-Kinase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg202

b:23.8
occ:1.00
 OG1 A:THR35 2.0 41.4 1.0
O A:HOH305 2.1 26.7 1.0
O2B A:GNP201 2.1 20.2 1.0
OG A:SER17 2.1 37.5 1.0
O2G A:GNP201 2.1 38.6 1.0
O A:HOH301 2.2 19.5 1.0
CB A:THR35 3.0 33.7 1.0
CB A:SER17 3.3 27.9 1.0
PB A:GNP201 3.3 31.1 1.0
PG A:GNP201 3.4 42.9 1.0
N3B A:GNP201 3.6 35.7 1.0
N A:SER17 3.8 36.6 1.0
OD2 A:ASP57 3.8 43.8 1.0
N A:THR35 3.9 39.5 1.0
CG2 A:THR35 4.0 33.7 1.0
CA A:THR35 4.0 37.7 1.0
O2A A:GNP201 4.1 40.9 1.0
CA A:SER17 4.1 30.4 1.0
O3G A:GNP201 4.1 46.1 1.0
O1B A:GNP201 4.2 26.2 1.0
OD1 A:ASP57 4.2 42.1 1.0
O A:HOH316 4.4 38.8 1.0
CG A:ASP57 4.4 37.8 1.0
O3A A:GNP201 4.4 37.1 1.0
O A:THR58 4.5 26.6 1.0
O1G A:GNP201 4.5 60.1 1.0
PA A:GNP201 4.6 35.5 1.0
O1A A:GNP201 4.6 29.3 1.0
O A:ASP33 4.7 41.7 1.0
CB A:LYS16 4.7 32.8 1.0
CE A:LYS16 4.7 39.8 1.0
C A:PRO34 4.8 41.6 1.0
C A:LYS16 4.9 30.5 1.0
NZ A:LYS16 4.9 37.5 1.0

Reference:

T.Cookis, C.Mattos. Crystal Structure Reveals the Full Ras:Raf Interface and Advances Mechanistic Understanding of Raf Activation Biorxiv 2020.
DOI: 10.1101/2020.07.28.225938
Page generated: Wed Oct 2 21:52:56 2024

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