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Chlorine 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:

Magnesium (Mg) 2 atoms
Zinc (Zn) 6 atoms

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total 2 binding sites of Chlorine 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 Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 5xna

Go back to Chlorine Binding Sites List in 5xna
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl212

b:24.1
occ:1.00
ZN B:ZN203 2.2 18.3 1.0
NZ B:LYS114 3.3 48.5 1.0
NE2 A:HIS129 3.4 19.3 1.0
ND1 B:HIS129 3.5 15.8 1.0
CD2 A:HIS129 3.5 18.1 1.0
CL B:CL212 3.6 20.8 1.0
CG B:PRO131 3.8 28.7 1.0
CB B:HIS129 3.9 15.4 1.0
CG B:HIS129 4.1 17.6 1.0
O A:HOH369 4.3 21.2 0.4
CE B:LYS114 4.3 49.0 1.0
CB B:PRO131 4.3 27.6 1.0
CE1 B:HIS129 4.5 15.6 1.0
O A:HOH369 4.6 22.2 0.6
CE1 A:HIS129 4.7 17.8 1.0
CD B:LYS114 4.8 35.5 1.0
CD B:PRO131 4.8 21.7 1.0
CA B:PRO131 4.9 21.5 1.0
CG A:HIS129 4.9 16.3 1.0

Chlorine binding site 2 out of 2 in 5xna

Go back to Chlorine Binding Sites List in 5xna
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl212

b:20.8
occ:1.00
ZN B:ZN203 2.3 18.3 1.0
O A:HOH376 3.1 18.6 0.6
ND1 B:HIS129 3.6 15.8 1.0
NE2 A:HIS129 3.6 19.3 1.0
CL A:CL212 3.6 24.1 1.0
O B:LYS135 3.8 16.0 1.0
CA B:PRO131 3.8 21.5 1.0
CG2 B:VAL136 3.9 15.4 1.0
CB B:HIS129 3.9 15.4 1.0
N B:PRO131 4.0 20.8 1.0
CE1 A:HIS129 4.1 17.8 1.0
CG B:HIS129 4.1 17.6 1.0
O B:VAL130 4.1 20.3 1.0
C B:VAL130 4.1 16.2 1.0
N B:VAL130 4.2 15.6 1.0
N B:LYS135 4.2 21.4 1.0
C B:LYS135 4.3 17.5 1.0
C B:ASN134 4.4 22.6 0.4
CA B:ASN134 4.4 25.1 0.6
CB B:PRO131 4.4 27.6 1.0
CA B:HIS129 4.4 16.0 1.0
CA B:ASN134 4.5 25.2 0.4
CG B:PRO131 4.5 28.7 1.0
C B:ASN134 4.6 23.2 0.6
CE1 B:HIS129 4.6 15.6 1.0
CD2 A:HIS129 4.7 18.1 1.0
C B:HIS129 4.7 14.8 1.0
OD1 B:ASN134 4.7 31.9 0.6
CD B:PRO131 4.7 21.7 1.0
N B:VAL136 4.9 15.2 1.0
C B:PRO131 4.9 19.7 1.0
CA B:VAL130 4.9 15.8 1.0
CA B:LYS135 4.9 21.4 1.0
O B:ASN134 4.9 21.8 0.4
O B:PRO131 5.0 24.4 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: Sat Jul 12 10:43:29 2025

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