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Sodium in PDB 8h1g: The R406T Mutant Form of the Aquifex Aeolicus Mutl Endonuclease Domain

Protein crystallography data

The structure of The R406T Mutant Form of the Aquifex Aeolicus Mutl Endonuclease Domain, PDB code: 8h1g was solved by K.Fukui, T.Yano, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.81 / 1.43
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 35.582, 35.582, 167.825, 90, 90, 90
R / Rfree (%) 19.3 / 22.1

Other elements in 8h1g:

The structure of The R406T Mutant Form of the Aquifex Aeolicus Mutl Endonuclease Domain also contains other interesting chemical elements:

Cadmium (Cd) 4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the The R406T Mutant Form of the Aquifex Aeolicus Mutl Endonuclease Domain (pdb code 8h1g). 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 R406T Mutant Form of the Aquifex Aeolicus Mutl Endonuclease Domain, PDB code: 8h1g:

Sodium binding site 1 out of 1 in 8h1g

Go back to Sodium Binding Sites List in 8h1g
Sodium binding site 1 out of 1 in the The R406T Mutant Form of the Aquifex Aeolicus Mutl Endonuclease Domain


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of The R406T Mutant Form of the Aquifex Aeolicus Mutl Endonuclease Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na502

b:22.5
occ:1.00
OD2 A:ASP366 2.3 29.3 1.0
OD1 A:ASP366 2.7 27.9 1.0
O A:HOH658 2.8 21.6 1.0
CG A:ASP366 2.9 27.8 1.0
CB A:ASN368 4.2 28.2 1.0
CB A:ASP366 4.4 26.7 1.0
N A:LEU369 4.4 19.2 1.0
CB A:LEU369 4.7 20.6 1.0
ND2 A:ASN368 5.0 33.4 1.0

Reference:

K.Fukui, T.Yamamoto, T.Murakawa, S.Baba, T.Kumasaka, T.Yano. Catalytic Mechanism of the Zinc-Dependent Mutl Endonuclease Reaction. Life Sci Alliance V. 6 2023.
ISSN: ESSN 2575-1077
PubMed: 37487639
DOI: 10.26508/LSA.202302001
Page generated: Thu Dec 28 11:37:42 2023

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