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Magnesium in PDB 5e95: Crystal Structure of Mb(NS1)/H-Ras Complex

Protein crystallography data

The structure of Crystal Structure of Mb(NS1)/H-Ras Complex, PDB code: 5e95 was solved by R.R.Eguchi, F.Sha, A.Gupta, A.Koide, S.Koide, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.14 / 1.40
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 35.897, 36.276, 54.348, 86.30, 74.23, 85.20
R / Rfree (%) 16.3 / 19.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Mb(NS1)/H-Ras Complex (pdb code 5e95). 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 Mb(NS1)/H-Ras Complex, PDB code: 5e95:

Magnesium binding site 1 out of 1 in 5e95

Go back to Magnesium Binding Sites List in 5e95
Magnesium binding site 1 out of 1 in the Crystal Structure of Mb(NS1)/H-Ras Complex


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 Mb(NS1)/H-Ras Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg202

b:34.9
occ:1.00
O2B A:GDP201 2.7 8.7 1.0
O2A A:GDP201 3.0 12.1 1.0
O3A A:GDP201 3.5 7.6 1.0
PB A:GDP201 3.7 7.8 1.0
N A:GLY13 3.8 8.0 1.0
PA A:GDP201 3.8 9.0 1.0
CA A:GLY13 3.8 8.1 1.0
C5' A:GDP201 4.0 7.6 1.0
O3B A:GDP201 4.4 9.1 1.0
O5' A:GDP201 4.4 7.7 1.0
C A:GLY12 4.8 7.5 1.0
O A:HOH330 4.8 35.4 1.0
O1B A:GDP201 4.9 7.7 1.0

Reference:

R.Spencer-Smith, A.Koide, Y.Zhou, R.R.Eguchi, F.Sha, P.Gajwani, D.Santana, A.Gupta, M.Jacobs, E.Herrero-Garcia, J.Cobbert, H.Lavoie, M.Smith, T.Rajakulendran, E.Dowdell, M.N.Okur, I.Dementieva, F.Sicheri, M.Therrien, J.F.Hancock, M.Ikura, S.Koide, J.P.O'bryan. Inhibition of Ras Function Through Targeting An Allosteric Regulatory Site. Nat. Chem. Biol. V. 13 62 2017.
ISSN: ESSN 1552-4469
PubMed: 27820802
DOI: 10.1038/NCHEMBIO.2231
Page generated: Sun Sep 29 03:32:34 2024

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