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Sodium in PDB 5vxa: Structure of the Human MESH1-Nadph Complex

Enzymatic activity of Structure of the Human MESH1-Nadph Complex

All present enzymatic activity of Structure of the Human MESH1-Nadph Complex:
3.1.7.2;

Protein crystallography data

The structure of Structure of the Human MESH1-Nadph Complex, PDB code: 5vxa was solved by J.Rose, P.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.07 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.780, 80.370, 114.460, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 20.6

Other elements in 5vxa:

The structure of Structure of the Human MESH1-Nadph Complex also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of the Human MESH1-Nadph Complex (pdb code 5vxa). 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 Structure of the Human MESH1-Nadph Complex, PDB code: 5vxa:

Sodium binding site 1 out of 1 in 5vxa

Go back to Sodium Binding Sites List in 5vxa
Sodium binding site 1 out of 1 in the Structure of the Human MESH1-Nadph Complex


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of the Human MESH1-Nadph Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na206

b:60.2
occ:1.00
O1N A:NDP202 2.2 52.5 1.0
O2A A:NDP202 2.2 49.9 0.9
PN A:NDP202 3.7 53.4 0.4
PA A:NDP202 3.7 45.0 1.0
O3 A:NDP202 4.1 50.6 0.9
O5B A:NDP202 4.3 38.1 0.8
C4B A:NDP202 4.4 29.0 1.0
O5D A:NDP202 4.5 52.1 0.7
O2N A:NDP202 4.8 55.9 0.7
C5B A:NDP202 4.8 33.4 1.0
NH2 A:ARG100 4.8 46.0 1.0
O1A A:NDP202 4.9 45.6 1.0
O3B A:NDP202 4.9 27.6 1.0

Reference:

C.-K.C.Ding, J.Rose, P.Zhou, J.-T.A.Chi. Mammalian Stringent-Like Response Mediated By the Cytosolic Nadph Phosphatase MESH1 Biorxiv 2018.
DOI: 10.1101/325266
Page generated: Mon Aug 18 02:53:12 2025

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