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Magnesium in PDB 1gua: Human RAP1A, Residues 1-167, Double Mutant (E30D,K31E) Complexed with Gppnhp and the Ras-Binding-Domain of Human C-RAF1, Residues 51-131

Protein crystallography data

The structure of Human RAP1A, Residues 1-167, Double Mutant (E30D,K31E) Complexed with Gppnhp and the Ras-Binding-Domain of Human C-RAF1, Residues 51-131, PDB code: 1gua was solved by N.Nassar, A.Wittinghofer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 44.500, 71.800, 100.300, 90.00, 90.00, 90.00
R / Rfree (%) 22 / n/a

Other elements in 1gua:

The structure of Human RAP1A, Residues 1-167, Double Mutant (E30D,K31E) Complexed with Gppnhp and the Ras-Binding-Domain of Human C-RAF1, Residues 51-131 also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Human RAP1A, Residues 1-167, Double Mutant (E30D,K31E) Complexed with Gppnhp and the Ras-Binding-Domain of Human C-RAF1, Residues 51-131 (pdb code 1gua). 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 Human RAP1A, Residues 1-167, Double Mutant (E30D,K31E) Complexed with Gppnhp and the Ras-Binding-Domain of Human C-RAF1, Residues 51-131, PDB code: 1gua:

Magnesium binding site 1 out of 1 in 1gua

Go back to Magnesium Binding Sites List in 1gua
Magnesium binding site 1 out of 1 in the Human RAP1A, Residues 1-167, Double Mutant (E30D,K31E) Complexed with Gppnhp and the Ras-Binding-Domain of Human C-RAF1, Residues 51-131


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human RAP1A, Residues 1-167, Double Mutant (E30D,K31E) Complexed with Gppnhp and the Ras-Binding-Domain of Human C-RAF1, Residues 51-131 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg171

b:10.4
occ:1.00
O3G A:GNP170 2.1 8.4 1.0
O A:HOH502 2.1 6.4 1.0
OG1 A:THR35 2.2 9.9 1.0
O A:HOH501 2.2 8.7 1.0
O2B A:GNP170 2.2 9.1 1.0
OG A:SER17 2.3 9.7 1.0
CB A:THR35 3.2 9.6 1.0
PB A:GNP170 3.3 8.7 1.0
PG A:GNP170 3.3 11.3 1.0
CB A:SER17 3.3 10.0 1.0
N3B A:GNP170 3.4 9.1 1.0
O1G A:GNP170 3.8 8.9 1.0
N A:THR35 3.8 10.5 1.0
N A:SER17 4.0 9.6 1.0
CA A:THR35 4.1 9.7 1.0
OD2 A:ASP57 4.2 9.8 1.0
O3A A:GNP170 4.2 7.6 1.0
CA A:SER17 4.2 9.8 1.0
OD1 A:ASP57 4.3 9.7 1.0
O A:HOH532 4.3 11.9 1.0
CG2 A:THR35 4.3 9.0 1.0
O1B A:GNP170 4.3 5.8 1.0
O2G A:GNP170 4.3 9.1 1.0
O1A A:GNP170 4.4 10.5 1.0
O A:THR58 4.4 10.7 1.0
PA A:GNP170 4.5 10.4 1.0
CG A:ASP57 4.6 10.4 1.0
O A:ASP33 4.6 11.9 1.0
O2A A:GNP170 4.7 9.2 1.0
C A:PRO34 4.8 11.4 1.0
CB A:LYS16 4.8 10.2 1.0
NZ A:LYS16 5.0 10.2 1.0
CE A:LYS16 5.0 8.9 1.0

Reference:

N.Nassar, G.Horn, C.Herrmann, C.Block, R.Janknecht, A.Wittinghofer. Ras/Rap Effector Specificity Determined By Charge Reversal. Nat.Struct.Biol. V. 3 723 1996.
ISSN: ISSN 1072-8368
PubMed: 8756332
DOI: 10.1038/NSB0896-723
Page generated: Mon Dec 14 05:58:23 2020

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