Magnesium in PDB 5xna: Crystal Structure of A Secretary Abundant Heat Soluble (Sahs) Protein From Ramazzottius Varieornatus (From Dimer Sample)

Protein crystallography data

The structure of Crystal Structure of A Secretary Abundant Heat Soluble (Sahs) Protein From Ramazzottius Varieornatus (From Dimer Sample), PDB code: 5xna was solved by Y.Fukuda, Y.Miura, E.Mizohata, T.Inoue, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.14 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.672, 57.799, 110.903, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 23.9

Other elements in 5xna:

The structure of Crystal Structure of A Secretary Abundant Heat Soluble (Sahs) Protein From Ramazzottius Varieornatus (From Dimer Sample) also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms
Zinc (Zn) 6 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of A Secretary Abundant Heat Soluble (Sahs) Protein From Ramazzottius Varieornatus (From Dimer Sample) (pdb code 5xna). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of A Secretary Abundant Heat Soluble (Sahs) Protein From Ramazzottius Varieornatus (From Dimer Sample), PDB code: 5xna:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 5xna

Go back to Magnesium Binding Sites List in 5xna
Magnesium binding site 1 out of 2 in the Crystal Structure of A Secretary Abundant Heat Soluble (Sahs) Protein From Ramazzottius Varieornatus (From Dimer Sample)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of A Secretary Abundant Heat Soluble (Sahs) Protein From Ramazzottius Varieornatus (From Dimer Sample) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg203

b:24.9
occ:1.00
OH A:TYR163 2.0 24.5 1.0
O2 A:SHV213 2.1 47.2 1.0
NE2 A:HIS72 2.1 24.9 1.0
O1 A:SHV213 2.3 43.9 1.0
C1 A:SHV213 2.4 45.3 1.0
OH A:TYR152 2.7 35.4 1.0
CD2 A:HIS72 3.0 23.3 1.0
CZ A:TYR163 3.1 23.3 1.0
CE1 A:HIS72 3.2 21.8 1.0
CD A:LYS150 3.7 35.1 1.0
NZ A:LYS150 3.7 42.3 1.0
C2 A:SHV213 3.7 49.0 1.0
CE1 A:TYR163 3.8 16.8 1.0
CG2 A:THR70 3.9 18.3 1.0
CE2 A:TYR163 3.9 17.2 1.0
CZ A:TYR152 3.9 35.2 1.0
CG A:HIS72 4.2 18.7 1.0
ND1 A:HIS72 4.2 19.7 1.0
CE A:LYS150 4.3 43.1 1.0
NH1 A:ARG161 4.3 36.3 1.0
CE2 A:TYR152 4.3 39.5 1.0
CD A:ARG161 4.7 29.4 1.0
CB A:THR70 4.8 20.4 1.0
C3 A:SHV213 4.9 55.1 1.0
CG A:LYS150 4.9 26.9 1.0

Magnesium binding site 2 out of 2 in 5xna

Go back to Magnesium Binding Sites List in 5xna
Magnesium binding site 2 out of 2 in the Crystal Structure of A Secretary Abundant Heat Soluble (Sahs) Protein From Ramazzottius Varieornatus (From Dimer Sample)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of A Secretary Abundant Heat Soluble (Sahs) Protein From Ramazzottius Varieornatus (From Dimer Sample) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg205

b:34.0
occ:1.00
OH B:TYR163 1.9 23.2 1.0
NE2 B:HIS72 2.3 21.7 1.0
OH B:TYR152 2.4 34.7 1.0
O B:ACY213 2.4 38.3 1.0
OXT B:ACY213 2.5 50.5 1.0
C B:ACY213 2.7 46.0 1.0
CZ B:TYR163 2.9 17.8 1.0
CD2 B:HIS72 3.1 27.6 1.0
CE1 B:HIS72 3.4 28.2 1.0
CZ B:TYR152 3.6 24.5 1.0
NZ B:LYS150 3.6 36.1 1.0
CE1 B:TYR163 3.7 18.2 1.0
CE2 B:TYR163 3.8 20.1 1.0
CD B:LYS150 3.8 28.2 1.0
CE2 B:TYR152 4.1 28.6 1.0
CG2 B:THR70 4.1 31.2 1.0
CH3 B:ACY213 4.2 43.1 1.0
CE B:LYS150 4.3 34.8 1.0
CG B:HIS72 4.3 21.9 1.0
NH1 B:ARG161 4.3 31.3 1.0
ND1 B:HIS72 4.4 20.5 1.0
CD B:ARG161 4.5 31.3 1.0
CE1 B:TYR152 4.7 20.5 1.0
CB B:THR70 4.9 30.3 1.0
CG B:LYS150 4.9 21.2 1.0
CD1 B:TYR163 5.0 17.6 1.0

Reference:

Y.Fukuda, Y.Miura, E.Mizohata, T.Inoue. Structural Insights Into A Secretory Abundant Heat-Soluble Protein From An Anhydrobiotic Tardigrade, Ramazzottius Varieornatus Febs Lett. V. 591 2458 2017.
ISSN: ISSN 1873-3468
PubMed: 28703282
DOI: 10.1002/1873-3468.12752
Page generated: Mon Dec 14 22:09:45 2020

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