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Magnesium in PDB 6wgh: Crystal Structure of Gdp-Bound Nras with Ten Residues Long Internal Tandem Duplication in the Switch II Region

Protein crystallography data

The structure of Crystal Structure of Gdp-Bound Nras with Ten Residues Long Internal Tandem Duplication in the Switch II Region, PDB code: 6wgh was solved by S.Dharmaiah, D.K.Simanshu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.89 / 1.65
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 40.460, 45.960, 89.080, 90.00, 99.77, 90.00
R / Rfree (%) 17.8 / 20.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Gdp-Bound Nras with Ten Residues Long Internal Tandem Duplication in the Switch II Region (pdb code 6wgh). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Gdp-Bound Nras with Ten Residues Long Internal Tandem Duplication in the Switch II Region, PDB code: 6wgh:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 6wgh

Go back to Magnesium Binding Sites List in 6wgh
Magnesium binding site 1 out of 3 in the Crystal Structure of Gdp-Bound Nras with Ten Residues Long Internal Tandem Duplication in the Switch II Region


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 Gdp-Bound Nras with Ten Residues Long Internal Tandem Duplication in the Switch II Region within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg201

b:23.4
occ:1.00
OA1 A:FLC203 2.0 21.1 0.8
O A:HOH326 2.0 29.9 1.0
OB1 A:FLC203 2.0 24.2 0.8
O A:HOH357 2.1 25.7 1.0
O A:HOH345 2.1 34.0 1.0
OHB A:FLC203 2.3 25.2 0.8
CBC A:FLC203 2.8 22.8 0.8
CB A:FLC203 2.9 25.1 0.8
CAC A:FLC203 3.0 21.0 0.8
CA A:FLC203 3.4 23.1 0.8
OB2 A:FLC203 4.0 21.5 0.8
OA2 A:FLC203 4.1 20.9 0.8
N A:ASP30 4.2 23.6 1.0
O A:PHE28 4.3 23.1 1.0
CB A:ASP30 4.3 24.1 1.0
NE2 A:HIS27 4.3 24.9 1.0
CG A:FLC203 4.3 27.5 0.8
OG2 A:FLC203 4.5 59.8 0.8
O B:HOH395 4.7 53.6 1.0
CE1 A:HIS27 4.8 29.4 1.0
CGC A:FLC203 4.8 47.0 0.8
CA A:VAL29 4.8 18.1 1.0
CA A:ASP30 4.9 25.4 1.0

Magnesium binding site 2 out of 3 in 6wgh

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Magnesium binding site 2 out of 3 in the Crystal Structure of Gdp-Bound Nras with Ten Residues Long Internal Tandem Duplication in the Switch II Region


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Gdp-Bound Nras with Ten Residues Long Internal Tandem Duplication in the Switch II Region within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg205

b:18.8
occ:1.00
O2B A:GDP202 2.0 17.9 1.0
OG A:SER17 2.1 17.6 1.0
O A:HOH311 2.1 22.1 1.0
O A:HOH306 2.2 16.8 1.0
O A:HOH323 2.2 19.7 1.0
O A:HOH321 2.2 19.0 1.0
CB A:SER17 3.1 17.2 1.0
PB A:GDP202 3.3 18.6 1.0
O1B A:GDP202 3.5 20.1 1.0
N A:SER17 3.9 17.3 1.0
O1A A:GDP202 4.1 21.2 1.0
CA A:SER17 4.1 18.5 1.0
OD2 A:ASP57 4.1 26.7 1.0
O3A A:GDP202 4.3 17.9 1.0
OD1 A:ASP57 4.3 24.2 1.0
O3B A:GDP202 4.3 19.4 1.0
O A:ILE36 4.4 19.4 1.0
O A:ASP33 4.4 20.5 1.0
CD2 A:TYR32 4.4 19.1 1.0
O A:THR58 4.5 22.8 1.0
PA A:GDP202 4.5 19.5 1.0
O A:PRO34 4.6 27.9 1.0
CA A:PRO34 4.6 20.6 1.0
CG A:ASP57 4.6 26.6 1.0
O2A A:GDP202 4.7 21.2 1.0
CE A:LYS16 4.9 20.9 1.0
C A:PRO34 4.9 20.7 1.0
O A:TYR32 4.9 21.1 1.0
CB A:LYS16 4.9 19.1 1.0
C A:LYS16 5.0 19.4 1.0

Magnesium binding site 3 out of 3 in 6wgh

Go back to Magnesium Binding Sites List in 6wgh
Magnesium binding site 3 out of 3 in the Crystal Structure of Gdp-Bound Nras with Ten Residues Long Internal Tandem Duplication in the Switch II Region


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Gdp-Bound Nras with Ten Residues Long Internal Tandem Duplication in the Switch II Region within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg201

b:16.5
occ:1.00
O2B B:GDP202 2.0 15.3 1.0
O B:HOH330 2.0 17.8 1.0
OG B:SER17 2.0 18.7 1.0
O B:HOH316 2.1 22.0 1.0
O B:HOH315 2.1 19.9 1.0
O B:HOH308 2.2 18.0 1.0
CB B:SER17 3.2 17.3 1.0
PB B:GDP202 3.3 16.5 1.0
O3B B:GDP202 3.5 17.9 1.0
N B:SER17 4.0 16.2 1.0
O2A B:GDP202 4.1 19.3 1.0
CA B:SER17 4.1 14.7 1.0
OD2 B:ASP57 4.2 24.7 1.0
O B:PRO34 4.2 21.4 1.0
OD1 B:ASP57 4.3 24.6 1.0
O B:ASP33 4.3 21.7 1.0
O1B B:GDP202 4.3 18.2 1.0
O B:ILE36 4.3 23.8 1.0
O3A B:GDP202 4.3 16.1 1.0
CD2 B:TYR32 4.4 19.1 1.0
O B:THR58 4.5 22.8 1.0
CA B:PRO34 4.6 18.4 1.0
PA B:GDP202 4.6 18.8 1.0
CG B:ASP57 4.6 27.4 1.0
C B:PRO34 4.7 22.5 1.0
O1A B:GDP202 4.7 19.4 1.0
CB B:LYS16 4.9 15.2 1.0
CE2 B:TYR32 4.9 21.6 1.0
CE B:LYS16 5.0 18.4 1.0
CB B:ALA59 5.0 27.8 1.0

Reference:

S.Dharmaiah, D.K.Simanshu. Ras Internal Tandem Duplication Disrupts Gtpase-Activating Protein (Gap) Binding to Activate Oncogenic Signaling J.Biol.Chem. 2020.
ISSN: ESSN 1083-351X
Page generated: Tue Oct 1 22:58:06 2024

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