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Sodium in PDB 3o7w: The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1

Protein crystallography data

The structure of The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1, PDB code: 3o7w was solved by M.L.Tsai, N.Cronin, S.Djordjevic, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.53 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.086, 63.296, 81.770, 90.00, 90.00, 90.00
R / Rfree (%) 20.5 / 26.5

Sodium Binding Sites:

The binding sites of Sodium atom in the The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1 (pdb code 3o7w). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1, PDB code: 3o7w:

Sodium binding site 1 out of 1 in 3o7w

Go back to Sodium Binding Sites List in 3o7w
Sodium binding site 1 out of 1 in the The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1

b:25.6
occ:1.00
N A:MET125 3.2 26.7 1.0
CB A:MET125 3.6 29.7 1.0
CD A:PRO124 3.7 24.8 1.0
N A:PRO124 3.8 24.9 1.0
CB A:PHE123 3.8 22.1 1.0
CG A:MET125 3.9 38.1 1.0
CB A:PRO124 3.9 27.2 1.0
CA A:MET125 4.0 28.0 1.0
CG A:PRO124 4.1 29.0 1.0
C A:PRO124 4.2 26.4 1.0
CD2 A:PHE123 4.2 25.6 1.0
CA A:PRO124 4.2 25.6 1.0
C A:PHE123 4.2 23.0 1.0
CG A:PHE123 4.3 21.3 1.0
CA A:PHE123 4.5 21.9 1.0
O A:PHE123 4.9 22.6 1.0

Reference:

M.L.Tsai, N.Cronin, S.Djordjevic. The Structure of Human Leucine Carboxyl Methyltransferase 1 That Regulates Protein Phosphatase PP2A Acta Crystallogr.,Sect.D V. 67 14 2011.
ISSN: ISSN 0907-4449
PubMed: 21206058
DOI: 10.1107/S0907444910042204
Page generated: Mon Oct 7 11:57:18 2024

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