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Calcium in PDB 3i3s: Crystal Structure of H-Ras with THR50 Replaced By Isoleucine

Protein crystallography data

The structure of Crystal Structure of H-Ras with THR50 Replaced By Isoleucine, PDB code: 3i3s was solved by L.Gremer, R.Dvorsky, T.Merbitz-Zahradnik, A.Wittinghofer, M.R.Ahmadian, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.86 / 1.36
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 89.210, 89.210, 134.640, 90.00, 90.00, 120.00
R / Rfree (%) 15.9 / 17.8

Other elements in 3i3s:

The structure of Crystal Structure of H-Ras with THR50 Replaced By Isoleucine also contains other interesting chemical elements:

Magnesium (Mg) 3 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of H-Ras with THR50 Replaced By Isoleucine (pdb code 3i3s). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of H-Ras with THR50 Replaced By Isoleucine, PDB code: 3i3s:

Calcium binding site 1 out of 1 in 3i3s

Go back to Calcium Binding Sites List in 3i3s
Calcium binding site 1 out of 1 in the Crystal Structure of H-Ras with THR50 Replaced By Isoleucine


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of H-Ras with THR50 Replaced By Isoleucine within 5.0Å range:
probe atom residue distance (Å) B Occ
R:Ca169

b:12.8
occ:1.00
O R:PHE28 2.3 14.0 1.0
OD1 R:ASP30 2.4 15.7 1.0
O R:HOH190 2.4 17.8 1.0
O R:HOH208 2.4 19.9 1.0
C R:PHE28 3.5 13.5 1.0
CG R:ASP30 3.6 15.1 1.0
N R:ASP30 4.1 13.1 1.0
CA R:VAL29 4.3 13.7 1.0
O R:HOH272 4.4 30.3 1.0
N R:VAL29 4.4 13.6 1.0
CB R:ASP30 4.4 14.7 1.0
O R:HOH185 4.5 21.7 1.0
OD2 R:ASP30 4.5 18.8 1.0
CA R:PHE28 4.6 13.1 1.0
N R:PHE28 4.7 13.5 1.0
C R:VAL29 4.7 13.6 1.0
CB R:PHE28 4.8 13.7 1.0
CA R:ASP30 4.9 13.8 1.0

Reference:

I.C.Cirstea, K.Kutsche, R.Dvorsky, L.Gremer, C.Carta, D.Horn, A.E.Roberts, F.Lepri, T.Merbitz-Zahradnik, R.Konig, C.P.Kratz, F.Pantaleoni, M.L.Dentici, V.A.Joshi, R.S.Kucherlapati, L.Mazzanti, S.Mundlos, M.A.Patton, M.C.Silengo, C.Rossi, G.Zampino, C.Digilio, L.Stuppia, E.Seemanova, L.A.Pennacchio, B.D.Gelb, B.Dallapiccola, A.Wittinghofer, M.R.Ahmadian, M.Tartaglia, M.Zenker. A Restricted Spectrum of Nras Mutations Causes Noonan Syndrome. Nat.Genet. V. 42 27 2010.
ISSN: ISSN 1061-4036
PubMed: 19966803
DOI: 10.1038/NG.497
Page generated: Sat Dec 12 04:14:59 2020

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