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Chlorine in PDB 6tt4: Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.

Enzymatic activity of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.

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

Protein crystallography data

The structure of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat., PDB code: 6tt4 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) 64.01 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 74.371, 78.825, 89.686, 92.43, 105.97, 114.60
R / Rfree (%) 18.2 / 22.2

Other elements in 6tt4:

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

Zinc (Zn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat. (pdb code 6tt4). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat., PDB code: 6tt4:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 6tt4

Go back to Chlorine Binding Sites List in 6tt4
Chlorine binding site 1 out of 2 in the Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl710

b:27.1
occ:1.00
 HE A:ARG500 2.4 30.5 1.0
HH A:TYR202 2.4 32.7 1.0
HB3 A:ARG500 2.8 33.1 1.0
HH21 A:ARG500 2.8 30.8 1.0
O A:HOH1107 3.0 28.5 1.0
HB2 A:PRO497 3.0 30.1 1.0
H A:ARG500 3.1 30.8 1.0
HE2 A:TYR202 3.1 35.0 1.0
OH A:TYR202 3.2 27.3 1.0
HG22 A:ILE499 3.2 32.0 1.0
HB2 A:PRO385 3.2 34.0 1.0
NE A:ARG500 3.2 25.4 1.0
HG2 A:PRO385 3.2 35.2 1.0
HE3 A:TRP201 3.3 36.3 1.0
HZ3 A:TRP201 3.3 35.6 1.0
NH2 A:ARG500 3.5 25.7 1.0
HG23 A:ILE499 3.6 32.0 1.0
CB A:ARG500 3.6 27.6 1.0
HG2 A:ARG500 3.7 30.9 1.0
N A:ARG500 3.7 25.7 1.0
HB3 A:PRO497 3.8 30.1 1.0
CE2 A:TYR202 3.8 29.2 1.0
CG2 A:ILE499 3.8 26.6 1.0
CB A:PRO497 3.8 25.1 1.0
CZ A:ARG500 3.9 28.1 1.0
CB A:PRO385 3.9 28.3 1.0
CE3 A:TRP201 3.9 30.3 1.0
CZ3 A:TRP201 3.9 29.7 1.0
CZ A:TYR202 3.9 27.5 1.0
CG A:PRO385 4.0 29.3 1.0
CG A:ARG500 4.0 25.8 1.0
HB3 A:PRO385 4.1 34.0 1.0
CA A:ARG500 4.1 25.9 1.0
HA A:ARG500 4.1 31.1 1.0
CD A:ARG500 4.2 27.6 1.0
HG21 A:ILE499 4.3 32.0 1.0
HH22 A:ARG500 4.3 30.8 1.0
H A:ILE499 4.3 28.8 1.0
HG2 A:PRO497 4.3 31.7 1.0
HB2 A:ARG500 4.4 33.1 1.0
HD2 A:PRO385 4.6 36.8 1.0
N A:ILE499 4.6 24.0 1.0
HG3 A:PRO385 4.6 35.2 1.0
C A:ILE499 4.7 23.9 1.0
CG A:PRO497 4.7 26.4 1.0
HD2 A:ARG500 4.8 33.2 1.0
C A:PRO497 4.8 26.4 1.0
O A:HOH1069 4.8 27.9 1.0
HD3 A:ARG500 4.9 33.2 1.0
CD A:PRO385 4.9 30.7 1.0
HB3 A:TRP198 5.0 34.5 1.0
CA A:PRO497 5.0 24.8 1.0
HG3 A:ARG500 5.0 30.9 1.0

Chlorine binding site 2 out of 2 in 6tt4

Go back to Chlorine Binding Sites List in 6tt4
Chlorine binding site 2 out of 2 in the Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl712

b:26.1
occ:1.00
 HE B:ARG500 2.3 28.0 1.0
HH B:TYR202 2.5 30.8 1.0
HB3 B:ARG500 2.7 28.6 1.0
HH21 B:ARG500 2.8 33.9 1.0
HB2 B:PRO497 2.9 28.4 1.0
NE B:ARG500 3.1 23.3 1.0
O B:HOH1118 3.1 29.5 1.0
HB2 B:PRO385 3.2 32.5 1.0
H B:ARG500 3.2 28.6 1.0
HE2 B:TYR202 3.2 33.9 1.0
HG2 B:PRO385 3.2 34.0 1.0
HE3 B:TRP201 3.3 41.0 1.0
OH B:TYR202 3.3 25.7 1.0
HZ3 B:TRP201 3.3 36.7 1.0
HG21 B:ILE499 3.3 31.3 1.0
NH2 B:ARG500 3.5 28.2 1.0
CB B:ARG500 3.6 23.9 1.0
HG22 B:ILE499 3.6 31.3 1.0
CB B:PRO497 3.7 23.6 1.0
HB3 B:PRO497 3.7 28.4 1.0
CZ B:ARG500 3.8 29.1 1.0
N B:ARG500 3.8 23.8 1.0
HG2 B:ARG500 3.8 26.5 1.0
CB B:PRO385 3.8 27.1 1.0
CE2 B:TYR202 3.9 28.2 1.0
CG2 B:ILE499 3.9 26.1 1.0
CG B:PRO385 4.0 28.4 1.0
CE3 B:TRP201 4.0 34.2 1.0
CZ3 B:TRP201 4.0 30.6 1.0
HB3 B:PRO385 4.0 32.5 1.0
CG B:ARG500 4.0 22.1 1.0
CZ B:TYR202 4.1 27.5 1.0
HG2 B:PRO497 4.1 31.3 1.0
CA B:ARG500 4.1 23.9 1.0
CD B:ARG500 4.2 26.1 1.0
HA B:ARG500 4.2 28.7 1.0
HB2 B:ARG500 4.3 28.6 1.0
HH22 B:ARG500 4.3 33.9 1.0
HG23 B:ILE499 4.4 31.3 1.0
CG B:PRO497 4.5 26.1 1.0
HD2 B:PRO385 4.5 32.2 1.0
H B:ILE499 4.6 27.7 1.0
HG3 B:PRO385 4.6 34.0 1.0
HD3 B:ARG500 4.7 31.4 1.0
HD2 B:ARG500 4.8 31.4 1.0
C B:PRO497 4.8 25.7 1.0
C B:ILE499 4.8 23.9 1.0
N B:ILE499 4.8 23.1 1.0
CD B:PRO385 4.8 26.9 1.0
CA B:PRO497 4.9 23.5 1.0
O B:HOH1022 4.9 26.7 1.0
O B:PRO497 5.0 22.9 1.0
N B:TYR498 5.0 23.2 1.0
H B:TYR498 5.0 27.9 1.0
HG3 B:ARG500 5.0 26.5 1.0

Reference:

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
Page generated: Mon Jul 29 15:35:37 2024

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