Zinc 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:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc 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 Zinc atom.
In total 2 binding sites of Zinc where determined in the Angiotensin Converting Enzyme N Domain Glycsoylation Mutant (NDOM389) in Complex with RXP407, PDB code: 3nxq:
Jump to Zinc binding site number: 1; 2;

Zinc 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 Zinc with other atoms in the Zn 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:Zn650 b:24.0 occ:1.00 NE2 A:HIS361 2.0 23.5 1.0 NE2 A:HIS365 2.1 21.4 1.0 OE1 A:GLU389 2.1 24.6 1.0 O3 A:RX4700 2.2 25.1 1.0 O4 A:RX4700 2.4 25.0 1.0 P1 A:RX4700 2.7 24.0 1.0 CE1 A:HIS361 2.9 24.4 1.0 CD2 A:HIS361 3.0 24.3 1.0 CE1 A:HIS365 3.0 22.1 1.0 CD A:GLU389 3.0 24.4 1.0 CD2 A:HIS365 3.1 21.5 1.0 OE2 A:GLU389 3.3 24.0 1.0 ND1 A:HIS361 4.0 23.9 1.0 NAW A:RX4700 4.0 26.7 1.0 CG A:HIS361 4.1 23.3 1.0 CBG A:RX4700 4.1 24.8 1.0 CAT A:RX4700 4.1 22.8 1.0 ND1 A:HIS365 4.1 21.2 1.0 CG A:HIS365 4.2 21.1 1.0 CBD A:RX4700 4.2 21.7 1.0 CE2 A:TYR501 4.3 17.9 1.0 CG A:GLU389 4.4 24.3 1.0 OH A:TYR501 4.5 19.8 1.0 O A:HOH666 4.6 29.7 1.0 CA A:GLU389 4.6 24.3 1.0 CBB A:RX4700 4.7 29.3 1.0 CB A:GLU389 4.8 24.4 1.0 OE1 A:GLU362 4.8 27.5 1.0 OE2 A:GLU362 4.8 29.5 1.0 CAR A:RX4700 4.9 31.9 1.0 CZ A:TYR501 4.9 18.6 1.0 CBA A:RX4700 4.9 21.8 1.0

Zinc 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 Zinc with other atoms in the Zn 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:Zn650 b:21.7 occ:1.00 OE1 B:GLU389 2.0 20.4 1.0 NE2 B:HIS365 2.0 22.6 1.0 NE2 B:HIS361 2.0 21.8 1.0 O3 B:RX4700 2.2 21.9 1.0 O4 B:RX4700 2.3 20.3 1.0 P1 B:RX4700 2.7 19.6 1.0 CE1 B:HIS365 2.9 23.3 1.0 CD B:GLU389 3.0 23.6 1.0 CD2 B:HIS361 3.0 21.5 1.0 CE1 B:HIS361 3.0 22.4 1.0 CD2 B:HIS365 3.0 22.7 1.0 OE2 B:GLU389 3.3 23.5 1.0 NAW B:RX4700 4.0 23.2 1.0 CBG B:RX4700 4.0 22.1 1.0 CAT B:RX4700 4.0 21.5 1.0 ND1 B:HIS361 4.1 22.6 1.0 ND1 B:HIS365 4.1 23.2 1.0 CG B:HIS361 4.1 22.1 1.0 CG B:HIS365 4.2 22.5 1.0 CE2 B:TYR501 4.2 19.6 1.0 CBD B:RX4700 4.2 20.3 1.0 O B:HOH769 4.2 18.3 1.0 CG B:GLU389 4.3 23.9 1.0 OH B:TYR501 4.3 21.7 1.0 CA B:GLU389 4.6 24.7 1.0 OE2 B:GLU362 4.7 24.9 1.0 CBB B:RX4700 4.7 27.6 1.0 CB B:GLU389 4.7 24.9 1.0 CZ B:TYR501 4.8 20.2 1.0 CAR B:RX4700 4.8 30.3 1.0 OE1 B:GLU362 4.8 25.0 1.0 CBA B:RX4700 4.9 20.2 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