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Magnesium in PDB 1em9: Rous Sarcoma Virus Capsid Protein: N-Terminal Domain

Protein crystallography data

The structure of Rous Sarcoma Virus Capsid Protein: N-Terminal Domain, PDB code: 1em9 was solved by R.L.Kingston, T.Fitzon-Ostendorp, E.Z.Eisenmesser, G.W.Schatz, V.M.Vogt, C.B.Post, M.G.Rossmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.50 / 2.05
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.500, 64.500, 108.900, 90.00, 90.00, 90.00
R / Rfree (%) 24.7 / 27.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Rous Sarcoma Virus Capsid Protein: N-Terminal Domain (pdb code 1em9). 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 Rous Sarcoma Virus Capsid Protein: N-Terminal Domain, PDB code: 1em9:

Magnesium binding site 1 out of 1 in 1em9

Go back to Magnesium Binding Sites List in 1em9
Magnesium binding site 1 out of 1 in the Rous Sarcoma Virus Capsid Protein: N-Terminal Domain


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Rous Sarcoma Virus Capsid Protein: N-Terminal Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg306

b:37.2
occ:1.00
O B:HOH304 2.1 30.5 1.0
O B:HOH305 2.2 25.7 1.0
O A:HOH303 2.2 26.5 1.0
OD1 A:ASP71 2.2 29.4 1.0
OD1 B:ASP71 2.2 30.3 1.0
O A:HOH302 2.5 46.8 1.0
CG A:ASP71 3.1 30.5 1.0
CG B:ASP71 3.1 31.5 1.0
OD2 A:ASP71 3.3 30.2 1.0
OD2 B:ASP71 3.4 29.3 1.0
O A:ALA67 4.3 27.9 1.0
O B:ALA67 4.3 27.8 1.0
CB B:ASP71 4.5 29.0 1.0
CB A:ASP71 4.5 25.0 1.0
N B:ASP71 4.8 25.5 1.0
CA B:ASP71 4.8 29.1 1.0
N A:ASP71 4.9 25.1 1.0
CA A:ASP71 4.9 24.2 1.0

Reference:

R.L.Kingston, T.Fitzon-Ostendorp, E.Z.Eisenmesser, G.W.Schatz, V.M.Vogt, C.B.Post, M.G.Rossmann. Structure and Self-Association of the Rous Sarcoma Virus Capsid Protein. Structure Fold.Des. V. 8 617 2000.
ISSN: ISSN 0969-2126
PubMed: 10873863
DOI: 10.1016/S0969-2126(00)00148-9
Page generated: Mon Dec 14 05:52:30 2020

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