Chlorine in PDB 3nxq: Angiotensin Converting Enzyme N Domain Glycsoylation Mutant (NDOM389) in Complex with RXP407

All present enzymatic activity of Angiotensin Converting Enzyme N Domain Glycsoylation Mutant (NDOM389) in Complex with RXP407:
3.4.15.1;

The structure of Angiotensin Converting Enzyme N Domain Glycsoylation Mutant (NDOM389) in Complex with RXP407, PDB code: 3nxq was solved by C.S.Anthony, H.R.Corradi, S.L.U.Schwager, P.Redelinghuys, D.Georgiadis, V.Dive, K.R.Acharya, E.D.Sturrock, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.81 / 1.99
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	72.882, 76.685, 82.646, 88.63, 64.17, 75.70
R / Rfree (%)	19.4 / 23.7

The structure of Angiotensin Converting Enzyme N Domain Glycsoylation Mutant (NDOM389) in Complex with RXP407 also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Chlorine atom in the Angiotensin Converting Enzyme N Domain Glycsoylation Mutant (NDOM389) in Complex with RXP407 (pdb code 3nxq). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Angiotensin Converting Enzyme N Domain Glycsoylation Mutant (NDOM389) in Complex with RXP407, PDB code: 3nxq:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Angiotensin Converting Enzyme N Domain Glycsoylation Mutant (NDOM389) in Complex with RXP407


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Angiotensin Converting Enzyme N Domain Glycsoylation Mutant (NDOM389) in Complex with RXP407 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl900 b:23.6 occ:1.00 O A:HOH751 2.9 18.5 1.0 OH A:TYR202 3.0 27.3 1.0 NE A:ARG500 3.2 20.4 1.0 NH2 A:ARG500 3.6 22.7 1.0 CB A:PRO497 3.6 23.5 1.0 CB A:ARG500 3.6 19.4 1.0 N A:ARG500 3.7 20.0 1.0 CE1 A:TYR202 3.7 29.1 1.0 CB A:PRO385 3.8 27.1 1.0 CG2 A:ILE499 3.8 21.1 1.0 CZ A:TYR202 3.8 29.2 1.0 CZ A:ARG500 3.9 22.4 1.0 CG A:PRO385 4.0 27.5 1.0 CE3 A:TRP201 4.0 36.2 1.0 CA A:ARG500 4.1 19.6 1.0 CG A:ARG500 4.1 20.2 1.0 CZ3 A:TRP201 4.1 36.8 1.0 CD A:ARG500 4.3 21.5 1.0 CG A:PRO497 4.4 24.2 1.0 C A:PRO497 4.6 22.4 1.0 C A:ILE499 4.7 20.4 1.0 N A:ILE499 4.7 20.8 1.0 CA A:PRO497 4.7 23.4 1.0 O A:PRO497 4.8 21.6 1.0 O A:HOH758 4.9 12.1 1.0 N A:TYR498 4.9 21.5 1.0 CA A:ILE499 5.0 20.7 1.0 CB A:ILE499 5.0 20.7 1.0

Chlorine binding site 2 out of 2 in the Angiotensin Converting Enzyme N Domain Glycsoylation Mutant (NDOM389) in Complex with RXP407


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Angiotensin Converting Enzyme N Domain Glycsoylation Mutant (NDOM389) in Complex with RXP407 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl900 b:28.8 occ:1.00 O B:HOH754 3.0 26.8 1.0 OH B:TYR202 3.0 31.2 1.0 NE B:ARG500 3.2 24.5 1.0 NH2 B:ARG500 3.5 25.3 1.0 CB B:PRO497 3.6 25.3 1.0 CE1 B:TYR202 3.7 33.4 1.0 CB B:ARG500 3.7 21.7 1.0 CB B:PRO385 3.7 27.9 1.0 CZ B:TYR202 3.8 33.1 1.0 N B:ARG500 3.8 21.9 1.0 CZ B:ARG500 3.8 25.4 1.0 CG2 B:ILE499 3.8 22.4 1.0 CG B:PRO385 3.9 28.9 1.0 CE3 B:TRP201 4.0 37.7 1.0 CG B:ARG500 4.1 22.2 1.0 CZ3 B:TRP201 4.1 37.3 1.0 CA B:ARG500 4.2 21.9 1.0 CD B:ARG500 4.2 24.3 1.0 CG B:PRO497 4.3 26.4 1.0 N B:ILE499 4.7 22.0 1.0 C B:PRO497 4.7 24.2 1.0 C B:ILE499 4.7 22.3 1.0 O B:HOH761 4.8 22.4 1.0 CA B:PRO497 4.8 25.0 1.0 CD B:PRO385 4.9 29.0 1.0 N B:TYR498 4.9 23.1 1.0 CD1 B:TYR202 4.9 34.0 1.0 O B:PRO497 5.0 23.8 1.0

C.S.Anthony, H.R.Corradi, S.L.Schwager, P.Redelinghuys, D.Georgiadis, V.Dive, K.R.Acharya, E.D.Sturrock. The N Domain of Human Angiotensin-I-Converting Enzyme: the Role of N-Glycosylation and the Crystal Structure in Complex with An N Domain-Specific Phosphinic Inhibitor, RXP407. J.Biol.Chem. V. 285 35685 2010.
ISSN: ISSN 0021-9258
PubMed: 20826823
DOI: 10.1074/JBC.M110.167866