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Chlorine in PDB 6eqx: X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba

Enzymatic activity of X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba

All present enzymatic activity of X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba:
3.4.21.75;

Protein crystallography data

The structure of X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba, PDB code: 6eqx was solved by S.O.Dahms, M.E.Than, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.16 / 1.99
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 131.805, 131.805, 155.347, 90.00, 90.00, 120.00
R / Rfree (%) 16.2 / 18.4

Other elements in 6eqx:

The structure of X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba 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 X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba (pdb code 6eqx). 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 X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba, PDB code: 6eqx:

Chlorine binding site 1 out of 1 in 6eqx

Go back to Chlorine Binding Sites List in 6eqx
Chlorine binding site 1 out of 1 in the X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Structure of the Proprotein Convertase Furin Bound with the Competitive Inhibitor Arg-Arg-Arg-Val-Arg-Amba within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl608

b:24.0
occ:1.00
 NZ A:LYS449 3.0 13.2 1.0
OH A:TYR571 3.2 19.2 1.0
O A:HOH800 3.5 28.0 1.0
OH A:TYR313 3.5 28.0 1.0
CE A:LYS449 3.8 14.3 1.0
CE1 A:TYR571 3.8 15.3 1.0
CE2 A:PHE275 3.8 40.2 1.0
CD A:LYS449 3.9 18.1 1.0
CZ A:TYR571 4.0 14.2 1.0
CZ A:PHE275 4.1 42.6 1.0
O A:HOH921 4.5 21.0 1.0
CZ A:TYR313 4.9 21.6 1.0
CD2 A:PHE275 5.0 40.9 1.0

Reference:

S.O.Dahms, K.Hardes, T.Steinmetzer, M.E.Than. X-Ray Structures of the Proprotein Convertase Furin Bound with Substrate Analogue Inhibitors Reveal Substrate Specificity Determinants Beyond the S4 Pocket. Biochemistry V. 57 925 2018.
ISSN: ISSN 1520-4995
PubMed: 29314830
DOI: 10.1021/ACS.BIOCHEM.7B01124
Page generated: Sat Jul 12 13:34:16 2025

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