Chlorine in PDB 5l6q: Refolded Al Protein From Cardiac Amyloidosis

Protein crystallography data

The structure of Refolded Al Protein From Cardiac Amyloidosis, PDB code: 5l6q was solved by K.Annamalai, F.Liberta, M.-T.Vielberg, H.Lilie, K.-H.Guehrs, A.Schierhorn, R.Koehler, A.Schmidt, C.Haupt, O.Hegenbart, S.Schoenland, M.Groll, M.Faendrich, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.40
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 58.020, 105.810, 34.750, 90.00, 90.00, 90.00
R / Rfree (%) 14.7 / 18.2

Other elements in 5l6q:

The structure of Refolded Al Protein From Cardiac Amyloidosis also contains other interesting chemical elements:

Zinc (Zn) 7 atoms
Sodium (Na) 3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Refolded Al Protein From Cardiac Amyloidosis (pdb code 5l6q). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Refolded Al Protein From Cardiac Amyloidosis, PDB code: 5l6q:

Chlorine binding site 1 out of 1 in 5l6q

Go back to Chlorine Binding Sites List in 5l6q
Chlorine binding site 1 out of 1 in the Refolded Al Protein From Cardiac Amyloidosis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Refolded Al Protein From Cardiac Amyloidosis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl206

b:19.7
occ:1.00
ZN B:ZN203 2.2 20.4 1.0
OD1 B:ASP58 3.3 17.8 1.0
NH1 B:ARG59 3.6 15.1 1.0
O B:HOH379 3.6 23.9 1.0
N B:ARG59 3.6 11.6 1.0
CB B:PRO57 3.7 17.3 1.0
CB B:ARG59 3.8 13.7 1.0
CG B:ARG59 3.9 12.8 1.0
N B:ASP58 4.0 13.5 1.0
CD B:ARG59 4.2 14.3 1.0
CA B:ARG59 4.3 12.2 1.0
C B:PRO57 4.4 12.5 1.0
CA B:PRO57 4.4 13.9 1.0
CG B:ASP58 4.4 18.0 1.0
C B:ASP58 4.5 14.2 1.0
CZ B:ARG59 4.6 12.2 1.0
CA B:ASP58 4.7 14.1 1.0
O B:HOH323 4.8 32.5 1.0
NE2 B:GLN77 4.8 14.8 0.5
CG B:PRO57 4.9 17.5 1.0
NE B:ARG59 4.9 12.6 1.0

Reference:

K.Annamalai, F.Liberta, M.T.Vielberg, W.Close, H.Lilie, K.H.Guhrs, A.Schierhorn, R.Koehler, A.Schmidt, C.Haupt, U.Hegenbart, S.Schonland, M.Schmidt, M.Groll, M.Fandrich. Common Fibril Structures Imply Systemically Conserved Protein Misfolding Pathways in Vivo. Angew. Chem. Int. Ed. Engl. V. 56 7510 2017.
ISSN: ESSN 1521-3773
PubMed: 28544119
DOI: 10.1002/ANIE.201701761
Page generated: Sat Dec 12 12:01:14 2020

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