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Sodium in PDB 5o4h: Hcgc From Methanococcus Maripaludis Cocrystallized with Sam and Pyridinol

Protein crystallography data

The structure of Hcgc From Methanococcus Maripaludis Cocrystallized with Sam and Pyridinol, PDB code: 5o4h was solved by T.Wagner, L.Bai, T.Xu, X.Hu, U.Ermler, S.Shima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.85 / 1.75
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 73.168, 77.736, 100.991, 90.00, 110.87, 90.00
R / Rfree (%) 16.8 / 19.3

Sodium Binding Sites:

The binding sites of Sodium atom in the Hcgc From Methanococcus Maripaludis Cocrystallized with Sam and Pyridinol (pdb code 5o4h). 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 Hcgc From Methanococcus Maripaludis Cocrystallized with Sam and Pyridinol, PDB code: 5o4h:

Sodium binding site 1 out of 1 in 5o4h

Go back to Sodium Binding Sites List in 5o4h
Sodium binding site 1 out of 1 in the Hcgc From Methanococcus Maripaludis Cocrystallized with Sam and Pyridinol


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Hcgc From Methanococcus Maripaludis Cocrystallized with Sam and Pyridinol within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Na302

b:32.2
occ:1.00
O D:ASP148 2.6 27.6 1.0
O D:SER145 2.8 28.5 1.0
O D:LYS146 3.0 40.5 1.0
C D:LYS146 3.5 38.5 1.0
O D:HOH510 3.6 45.6 1.0
C D:ASP148 3.7 27.7 1.0
CA D:LYS146 3.9 32.8 1.0
C D:SER145 3.9 31.6 1.0
N D:ASP148 4.1 27.7 1.0
O D:HOH512 4.3 54.0 1.0
N D:LYS146 4.3 30.6 1.0
CA D:ASP148 4.4 26.4 1.0
N D:ILE147 4.5 35.1 1.0
O D:HOH564 4.5 35.5 1.0
C D:ILE147 4.6 34.0 1.0
CB D:ASP148 4.7 27.0 1.0
N D:ASN149 4.8 24.7 1.0
CA D:ILE147 5.0 34.8 1.0

Reference:

L.Bai, T.Wagner, T.Xu, X.Hu, U.Ermler, S.Shima. A Water-Bridged H-Bonding Network Contributes to the Catalysis of the Sam-Dependent C-Methyltransferase Hcgc. Angew. Chem. Int. Ed. Engl. V. 56 10806 2017.
ISSN: ESSN 1521-3773
PubMed: 28682478
DOI: 10.1002/ANIE.201705605
Page generated: Mon Oct 7 23:05:49 2024

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