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Magnesium in PDB 1agp: Three-Dimensional Structures and Properties of A Transforming and A Nontransforming Gly-12 Mutant of P21-H-Ras

Protein crystallography data

The structure of Three-Dimensional Structures and Properties of A Transforming and A Nontransforming Gly-12 Mutant of P21-H-Ras, PDB code: 1agp was solved by S.M.Franken, A.J.Scheidig, A.Wittinghofer, R.S.Goody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.30
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 69.910, 39.810, 56.100, 90.00, 107.40, 90.00
R / Rfree (%) 17.7 / n/a

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Three-Dimensional Structures and Properties of A Transforming and A Nontransforming Gly-12 Mutant of P21-H-Ras (pdb code 1agp). 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 Three-Dimensional Structures and Properties of A Transforming and A Nontransforming Gly-12 Mutant of P21-H-Ras, PDB code: 1agp:

Magnesium binding site 1 out of 1 in 1agp

Go back to Magnesium Binding Sites List in 1agp
Magnesium binding site 1 out of 1 in the Three-Dimensional Structures and Properties of A Transforming and A Nontransforming Gly-12 Mutant of P21-H-Ras


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Three-Dimensional Structures and Properties of A Transforming and A Nontransforming Gly-12 Mutant of P21-H-Ras within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg168

b:6.9
occ:1.00
O1G A:GNP167 2.4 5.6 1.0
O2B A:GNP167 2.4 4.0 1.0
OG1 A:THR35 2.6 10.8 1.0
OG A:SER17 2.6 3.3 1.0
HG A:SER17 2.6 0.0 1.0
O A:HOH172 2.7 4.6 1.0
CB A:THR35 3.1 12.6 1.0
H2 A:HOH172 3.2 0.0 1.0
O A:THR58 3.2 9.3 1.0
OD1 A:ASP57 3.4 10.2 1.0
HG1 A:THR35 3.4 0.0 1.0
OD2 A:ASP57 3.4 7.0 1.0
H A:SER17 3.5 0.0 1.0
H A:THR35 3.5 0.0 1.0
H1 A:HOH172 3.5 0.0 1.0
PG A:GNP167 3.5 7.6 1.0
PB A:GNP167 3.6 3.3 1.0
CG A:ASP57 3.7 7.5 1.0
HZ2 A:LYS16 3.8 0.0 1.0
CD A:LYS16 3.9 7.0 1.0
CB A:SER17 3.9 7.7 1.0
N A:SER17 3.9 10.3 1.0
N3B A:GNP167 4.0 5.5 1.0
CG2 A:THR35 4.1 12.0 1.0
HNB3 A:GNP167 4.1 0.0 1.0
N A:THR35 4.1 12.7 1.0
CB A:LYS16 4.1 4.7 1.0
O3G A:GNP167 4.2 9.8 1.0
CA A:THR35 4.3 12.0 1.0
O1B A:GNP167 4.3 4.5 1.0
CA A:SER17 4.3 9.0 1.0
CE A:LYS16 4.4 2.0 1.0
C A:THR58 4.4 6.9 1.0
NZ A:LYS16 4.5 2.6 1.0
CG A:LYS16 4.7 6.7 1.0
O2G A:GNP167 4.7 9.8 1.0
C A:LYS16 4.8 10.2 1.0
O3A A:GNP167 4.9 5.0 1.0
H A:GLY60 4.9 0.0 1.0
O2A A:GNP167 4.9 11.8 1.0
H A:LYS16 5.0 0.0 1.0
HZ1 A:LYS16 5.0 0.0 1.0
N A:THR58 5.0 5.0 1.0
H A:THR58 5.0 0.0 1.0
CA A:LYS16 5.0 8.2 1.0

Reference:

S.M.Franken, A.J.Scheidig, U.Krengel, H.Rensland, A.Lautwein, M.Geyer, K.Scheffzek, R.S.Goody, H.R.Kalbitzer, E.F.Pai, A.Wittinghofer. Three-Dimensional Structures and Properties of A Transforming and A Nontransforming Glycine-12 Mutant of P21H-Ras. Biochemistry V. 32 8411 1993.
ISSN: ISSN 0006-2960
PubMed: 8357792
DOI: 10.1021/BI00084A005
Page generated: Mon Dec 14 03:31:41 2020

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