Atomistry » Chlorine » PDB 5fs0-5fza » 5fwz
Atomistry »
  Chlorine »
    PDB 5fs0-5fza »
      5fwz »

Chlorine in PDB 5fwz: Fasciola Hepatica Calcium Binding Protein FHCABP2: Structure of the Dynein Light Chain-Like Domain. P41212 Mercury Derivative.

Protein crystallography data

The structure of Fasciola Hepatica Calcium Binding Protein FHCABP2: Structure of the Dynein Light Chain-Like Domain. P41212 Mercury Derivative., PDB code: 5fwz was solved by T.H.Nguyen, C.M.Thomas, D.J.Timson, M.J.Van Raaij, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.83 / 2.30
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 59.880, 59.880, 81.320, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 24.1

Other elements in 5fwz:

The structure of Fasciola Hepatica Calcium Binding Protein FHCABP2: Structure of the Dynein Light Chain-Like Domain. P41212 Mercury Derivative. also contains other interesting chemical elements:

Mercury (Hg) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Fasciola Hepatica Calcium Binding Protein FHCABP2: Structure of the Dynein Light Chain-Like Domain. P41212 Mercury Derivative. (pdb code 5fwz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Fasciola Hepatica Calcium Binding Protein FHCABP2: Structure of the Dynein Light Chain-Like Domain. P41212 Mercury Derivative., PDB code: 5fwz:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 5fwz

Go back to Chlorine Binding Sites List in 5fwz
Chlorine binding site 1 out of 2 in the Fasciola Hepatica Calcium Binding Protein FHCABP2: Structure of the Dynein Light Chain-Like Domain. P41212 Mercury Derivative.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Fasciola Hepatica Calcium Binding Protein FHCABP2: Structure of the Dynein Light Chain-Like Domain. P41212 Mercury Derivative. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1190

b:68.2
occ:1.00
SD A:MET143 3.2 42.1 1.0
CB A:CYS153 3.2 32.1 1.0
CB A:ALA183 3.3 23.7 1.0
HG A:HG1189 3.4 48.4 1.0
N A:LYS140 3.6 28.5 1.0
O A:GLN152 3.7 32.5 1.0
C A:MET139 3.8 28.7 1.0
CA A:CYS153 3.8 30.8 1.0
CA A:LYS140 3.8 29.5 1.0
SG A:CYS153 3.9 39.7 1.0
CB A:MET139 3.9 29.2 1.0
O A:MET139 4.0 27.4 1.0
C A:GLN152 4.2 29.6 1.0
CG A:MET143 4.3 34.3 1.0
N A:CYS153 4.3 29.3 1.0
CA A:ALA183 4.4 24.8 1.0
CB A:MET143 4.5 29.5 1.0
CB A:TRP151 4.5 28.8 1.0
CB A:LYS140 4.6 29.1 1.0
CA A:MET139 4.6 29.5 1.0
CE A:MET143 4.6 40.3 1.0
O A:LEU182 4.7 22.6 1.0
CE A:MET139 4.8 35.6 1.0
CE3 A:TRP151 4.9 28.6 1.0

Chlorine binding site 2 out of 2 in 5fwz

Go back to Chlorine Binding Sites List in 5fwz
Chlorine binding site 2 out of 2 in the Fasciola Hepatica Calcium Binding Protein FHCABP2: Structure of the Dynein Light Chain-Like Domain. P41212 Mercury Derivative.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Fasciola Hepatica Calcium Binding Protein FHCABP2: Structure of the Dynein Light Chain-Like Domain. P41212 Mercury Derivative. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1191

b:56.4
occ:1.00
ND1 A:HIS163 2.6 50.9 1.0
O A:MET162 3.4 38.9 1.0
CE1 A:HIS163 3.5 52.1 1.0
CG A:HIS163 3.6 46.8 1.0
CA A:HIS163 3.6 41.9 1.0
CB A:HIS163 3.8 43.5 1.0
C A:MET162 4.2 37.2 1.0
N A:HIS163 4.4 38.1 1.0
N A:PHE164 4.4 49.6 1.0
C A:HIS163 4.6 45.6 1.0
NE2 A:HIS163 4.6 51.2 1.0
CD2 A:HIS163 4.7 48.3 1.0

Reference:

T.H.Nguyen, C.M.Thomas, D.J.Timson, M.J.Van Raaij. Fasciola Hepatica Calcium-Binding Protein FHCABP2: Structure of the Dynein Light Chain-Like Domain. Parasitol. Res. V. 115 2879 2016.
ISSN: ISSN 1432-1955
PubMed: 27083189
DOI: 10.1007/S00436-016-5046-X
Page generated: Fri Jul 26 08:13:16 2024

Last articles

Ca in 8TCF
Ca in 8TE2
Ca in 8TB2
Ca in 8TAV
Ca in 8TAI
Ca in 8TAL
Ca in 8TAG
Ca in 8T2R
Ca in 8T2V
Ca in 8T7C
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy