Calcium in PDB 6tt3: Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6.

All present enzymatic activity of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6.:
3.4.15.1;

The structure of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6., PDB code: 6tt3 was solved by G.E.Cozier, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	75.11 / 1.70
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	73.617, 78.201, 83.789, 88.64, 64.35, 74.64
R / Rfree (%)	18.8 / 22.1

The structure of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6. also contains other interesting chemical elements:

Zinc	(Zn)	2 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Calcium atom in the Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6. (pdb code 6tt3). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6., PDB code: 6tt3:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca724 b:24.5 occ:0.78 O A:HOH920 2.3 28.6 1.0 O20 A:BJ2714 2.4 31.1 1.0 O A:HOH855 2.4 37.2 0.7 O22 A:BCN722 2.5 34.4 1.0 O6 A:BCN723 2.5 31.5 0.9 O4 A:BCN723 2.5 27.8 0.9 O21 A:BCN723 2.5 35.8 0.9 N1 A:BCN723 2.6 33.8 0.9 HO4 A:BCN723 2.8 33.4 0.9 HO6 A:BCN723 2.9 37.8 0.9 H62 A:BCN723 3.0 54.5 0.9 C6 A:BCN723 3.1 45.4 0.9 C2 A:BCN723 3.3 37.2 0.9 C5 A:BCN723 3.4 46.7 0.9 C3 A:BCN723 3.4 34.3 0.9 C4 A:BCN723 3.4 32.7 0.9 C2 A:BCN722 3.4 49.4 1.0 C18 A:BJ2714 3.4 22.5 1.0 C1 A:BCN723 3.4 39.4 0.9 O21 A:BCN722 3.6 36.6 1.0 H31 A:BCN723 3.7 41.2 0.9 H52 A:BCN723 3.8 56.0 0.9 H11 A:BCN723 3.8 47.3 0.9 H161 A:BJ2714 3.8 23.9 1.0 O19 A:BJ2714 3.9 26.6 1.0 H162 A:BJ2714 3.9 23.9 1.0 H42 A:BCN723 4.0 39.2 0.9 H61 A:BCN723 4.0 54.5 0.9 H41 A:BCN723 4.1 39.2 0.9 O A:HOH1113 4.1 40.3 1.0 H51 A:BCN723 4.1 56.0 0.9 H12 A:BCN723 4.2 47.3 0.9 H32 A:BCN723 4.2 41.2 0.9 N16 A:BJ2714 4.3 19.9 1.0 O A:HOH835 4.3 34.4 1.0 HZ A:PHE369 4.4 22.7 1.0 HE1 A:PHE369 4.5 25.3 1.0 O A:HOH906 4.5 39.1 1.0 O22 A:BCN723 4.5 35.7 0.9 H151 A:BJ2714 4.6 28.6 1.0 H61 A:BCN722 4.7 63.7 1.0 C17 A:BJ2714 4.7 21.1 1.0 C15 A:BJ2714 4.8 23.8 1.0 O A:HOH956 4.9 19.4 1.0 C1 A:BCN722 4.9 35.3 1.0 CZ A:PHE369 5.0 18.9 1.0 HE1 A:TYR338 5.0 33.0 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with SG6. within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca717 b:44.0 occ:1.00 O21 B:BCN716 2.2 41.6 1.0 O20 B:BJ2710 2.3 43.9 1.0 O1 B:PEG712 2.4 41.7 1.0 O B:HOH805 2.4 37.5 1.0 O2 B:PEG712 2.4 63.9 1.0 H41 B:PEG712 2.6 59.1 1.0 O B:HOH804 2.7 45.5 1.0 O4 B:PEG712 2.8 54.5 1.0 HO1 B:PEG712 2.8 50.1 1.0 C4 B:PEG712 2.9 49.2 1.0 C2 B:PEG712 3.0 58.3 1.0 H21 B:PEG712 3.0 70.0 1.0 C3 B:PEG712 3.1 56.5 1.0 C2 B:BCN716 3.2 61.5 1.0 C1 B:PEG712 3.2 52.0 1.0 HO4 B:PEG712 3.2 65.4 1.0 O22 B:BCN716 3.3 42.0 1.0 C18 B:BJ2710 3.4 31.2 1.0 H32 B:PEG712 3.4 67.8 1.0 H162 B:BJ2710 3.6 40.5 1.0 H12 B:PEG712 3.6 62.5 1.0 O19 B:BJ2710 3.8 38.1 1.0 H42 B:PEG712 3.9 59.1 1.0 H31 B:PEG712 3.9 67.8 1.0 H22 B:PEG712 3.9 70.0 1.0 H11 B:PEG712 4.0 62.5 1.0 HO1 B:EDO715 4.1 67.8 1.0 HZ B:PHE369 4.2 37.4 1.0 O B:HOH909 4.3 40.9 1.0 N16 B:BJ2710 4.4 33.8 1.0 HE1 B:PHE369 4.4 36.0 1.0 O1 B:EDO715 4.6 56.5 1.0 H161 B:BJ2710 4.6 40.5 1.0 C1 B:BCN716 4.6 55.7 1.0 H151 B:BJ2710 4.7 30.9 1.0 C17 B:BJ2710 4.7 33.0 1.0 H11 B:EDO715 4.8 78.3 1.0 CZ B:PHE369 4.8 31.1 1.0 C15 B:BJ2710 4.9 25.7 1.0 OH B:TYR338 4.9 56.2 1.0 CE1 B:PHE369 4.9 29.9 1.0 H11 B:BCN716 4.9 66.9 1.0 O B:HOH815 4.9 38.2 1.0

G.E.Cozier, L.Lubbe, E.D.Sturrock, K.R.Acharya. Ace-Domain Selectivity Extends Beyond Direct Interacting Residues at the Active Site. Biochem.J. 2020.
ISSN: ESSN 1470-8728
PubMed: 32195541
DOI: 10.1042/BCJ20200060