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Chlorine in PDB 5jxh: Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution.

Enzymatic activity of Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution.

All present enzymatic activity of Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution.:
3.4.21.75;

Protein crystallography data

The structure of Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution., PDB code: 5jxh was solved by S.O.Dahms, M.Arciniega, T.Steinmetzer, R.Huber, M.E.Than, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.14 / 2.00
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 131.790, 131.790, 155.578, 90.00, 90.00, 120.00
R / Rfree (%) 15.7 / 18.5

Other elements in 5jxh:

The structure of Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution. also contains other interesting chemical elements:

Calcium (Ca) 3 atoms
Sodium (Na) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution. (pdb code 5jxh). 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 Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution., PDB code: 5jxh:

Chlorine binding site 1 out of 1 in 5jxh

Go back to Chlorine Binding Sites List in 5jxh
Chlorine binding site 1 out of 1 in the Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure the Proprotein Convertase Furin in Complex with Meta- Guanidinomethyl-Phac-Rvr-Amba at 2.0 Angstrom Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl608

b:20.1
occ:1.00
NZ A:LYS449 3.2 16.2 1.0
OH A:TYR571 3.2 19.3 1.0
O A:HOH783 3.4 23.6 1.0
OH A:TYR313 3.7 24.1 1.0
CE A:LYS449 3.8 18.3 1.0
CE1 A:TYR571 3.8 18.2 1.0
CD A:LYS449 3.9 17.3 1.0
CZ A:TYR571 4.0 15.2 1.0
CE2 A:PHE275 4.2 19.6 0.5
O A:HOH1018 4.6 20.4 1.0
CZ A:PHE275 5.0 17.0 0.5

Reference:

S.O.Dahms, M.Arciniega, T.Steinmetzer, R.Huber, M.E.Than. Structure of the Unliganded Form of the Proprotein Convertase Furin Suggests Activation By A Substrate-Induced Mechanism. Proc.Natl.Acad.Sci.Usa V. 113 11196 2016.
ISSN: ESSN 1091-6490
PubMed: 27647913
DOI: 10.1073/PNAS.1613630113
Page generated: Sat Dec 12 11:54:54 2020

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