Chlorine in PDB 6qs1: Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb

Enzymatic activity of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb

All present enzymatic activity of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb:
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb, PDB code: 6qs1 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) 74.05 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 72.682, 77.070, 82.363, 88.86, 64.59, 75.03
R / Rfree (%) 20.2 / 23.2

Other elements in 6qs1:

The structure of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Zinc (Zn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb (pdb code 6qs1). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb, PDB code: 6qs1:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 6qs1

Go back to Chlorine Binding Sites List in 6qs1
Chlorine binding site 1 out of 4 in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb


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 Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl723

b:25.2
occ:1.00
 HH A:TYR202 2.4 28.4 1.0
HE A:ARG500 2.4 29.6 1.0
HB3 A:ARG500 2.7 29.1 1.0
HH21 A:ARG500 2.8 32.7 1.0
HB2 A:PRO497 2.9 28.3 1.0
HB2 A:PRO385 3.1 31.6 1.0
OH A:TYR202 3.1 23.6 1.0
O A:HOH1032 3.1 26.4 1.0
H A:ARG500 3.1 26.4 1.0
HG22 A:ILE499 3.1 28.8 1.0
HE2 A:TYR202 3.1 34.9 1.0
HE3 A:TRP201 3.2 38.9 1.0
NE A:ARG500 3.2 24.6 1.0
HG2 A:PRO385 3.2 31.1 1.0
HZ3 A:TRP201 3.3 37.7 1.0
NH2 A:ARG500 3.5 27.2 1.0
CB A:ARG500 3.6 24.2 1.0
CB A:PRO385 3.7 26.3 1.0
N A:ARG500 3.7 22.0 1.0
CB A:PRO497 3.7 23.5 1.0
HG2 A:ARG500 3.8 29.9 1.0
HB3 A:PRO497 3.8 28.3 1.0
HB3 A:PRO385 3.8 31.6 1.0
CE2 A:TYR202 3.8 29.1 1.0
CZ A:ARG500 3.8 26.8 1.0
CG2 A:ILE499 3.9 23.9 1.0
CE3 A:TRP201 3.9 32.4 1.0
HG23 A:ILE499 3.9 28.8 1.0
CZ A:TYR202 3.9 25.3 1.0
CZ3 A:TRP201 3.9 31.4 1.0
CG A:PRO385 3.9 25.9 1.0
CG A:ARG500 4.1 24.9 1.0
CA A:ARG500 4.1 22.8 1.0
HG2 A:PRO497 4.1 29.4 1.0
HA A:ARG500 4.1 27.3 1.0
HG21 A:ILE499 4.2 28.8 1.0
CD A:ARG500 4.2 24.8 1.0
HH22 A:ARG500 4.3 32.7 1.0
HB2 A:ARG500 4.3 29.1 1.0
H A:ILE499 4.4 29.3 1.0
HD2 A:PRO385 4.5 32.1 1.0
CG A:PRO497 4.5 24.5 1.0
HG3 A:PRO385 4.6 31.1 1.0
N A:ILE499 4.7 24.4 1.0
C A:ILE499 4.7 23.3 1.0
C A:PRO497 4.7 26.4 1.0
HD2 A:ARG500 4.8 29.8 1.0
CD A:PRO385 4.8 26.7 1.0
O A:HOH943 4.9 24.2 1.0
HD3 A:ARG500 4.9 29.8 1.0
CA A:PRO497 4.9 22.8 1.0
N A:TYR498 4.9 25.5 1.0
O A:PRO497 5.0 25.2 1.0
H A:TYR498 5.0 30.6 1.0

Chlorine binding site 2 out of 4 in 6qs1

Go back to Chlorine Binding Sites List in 6qs1
Chlorine binding site 2 out of 4 in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb


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 Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl724

b:36.1
occ:1.00
 HZ3 E:LYS8 2.2 45.9 0.8
H A:GLY382 2.2 34.3 1.0
HA A:PRO385 2.7 29.8 1.0
NZ E:LYS8 3.0 38.2 0.8
HB3 A:ARG381 3.0 44.4 1.0
O A:HOH948 3.0 32.4 1.0
N A:GLY382 3.1 28.6 1.0
HD2 A:HIS388 3.1 34.5 1.0
HZ1 E:LYS8 3.2 45.9 0.8
HE3 E:LYS8 3.4 44.7 0.8
HD3 A:ARG381 3.5 59.2 1.0
HA3 A:GLY382 3.5 36.8 1.0
HG3 A:PRO385 3.5 31.1 1.0
HB2 A:HIS388 3.5 31.8 1.0
HZ2 E:LYS8 3.6 45.9 0.8
CA A:PRO385 3.6 24.8 1.0
CE E:LYS8 3.7 37.2 0.8
CA A:GLY382 3.8 30.6 1.0
HA A:ARG381 3.8 39.3 1.0
H11 A:EDO711 3.8 61.4 1.0
CD2 A:HIS388 3.8 28.8 1.0
HE2 E:LYS8 3.8 44.7 0.8
CB A:ARG381 3.9 37.0 1.0
HB3 A:PRO385 3.9 31.6 1.0
N A:PRO385 4.0 25.5 1.0
C A:ARG381 4.0 29.4 1.0
CA A:ARG381 4.1 32.7 1.0
NE A:ARG381 4.1 49.8 1.0
HH11 A:ARG381 4.1 65.1 1.0
CZ A:ARG381 4.2 47.4 1.0
CD A:ARG381 4.2 49.3 1.0
CB A:PRO385 4.2 26.3 1.0
CG A:PRO385 4.2 25.9 1.0
NH1 A:ARG381 4.2 54.2 1.0
O A:ASN384 4.2 25.7 1.0
O A:GLY382 4.3 29.4 1.0
O E:HOH103 4.3 29.0 1.0
CB A:HIS388 4.3 26.4 1.0
C A:ASN384 4.4 28.2 1.0
CG A:HIS388 4.4 26.3 1.0
HE A:ARG381 4.5 59.8 1.0
C A:GLY382 4.5 30.6 1.0
HB2 A:ARG381 4.5 44.4 1.0
HH12 A:ARG381 4.6 65.1 1.0
HD3 A:PRO385 4.6 32.1 1.0
HB3 A:HIS388 4.6 31.8 1.0
CD A:PRO385 4.6 26.7 1.0
HA2 A:GLY382 4.6 36.8 1.0
CG A:ARG381 4.6 42.6 1.0
NH2 A:ARG381 4.7 46.6 1.0
C A:PRO385 4.8 25.5 1.0
H A:HIS388 4.8 29.8 1.0
C1 A:EDO711 4.8 51.2 1.0
H12 A:EDO711 4.8 61.4 1.0
O A:PRO385 4.9 25.5 1.0
NE2 A:HIS388 4.9 29.0 1.0

Chlorine binding site 3 out of 4 in 6qs1

Go back to Chlorine Binding Sites List in 6qs1
Chlorine binding site 3 out of 4 in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl715

b:32.8
occ:1.00
 HE B:ARG500 2.3 38.4 1.0
HH B:TYR202 2.4 37.9 1.0
HB3 B:ARG500 2.7 34.7 1.0
HH21 B:ARG500 2.8 41.1 1.0
HB2 B:PRO497 2.8 33.3 1.0
O B:HOH979 3.0 35.9 1.0
HG22 B:ILE499 3.1 32.3 1.0
H B:ARG500 3.1 32.9 1.0
HB2 B:PRO385 3.1 44.7 1.0
HE3 B:TRP201 3.2 49.3 1.0
OH B:TYR202 3.2 31.6 1.0
HE1 B:TYR202 3.2 41.9 1.0
NE B:ARG500 3.2 31.9 1.0
HZ3 B:TRP201 3.2 45.3 1.0
HG2 B:PRO385 3.2 44.3 1.0
NH2 B:ARG500 3.5 34.2 1.0
CB B:ARG500 3.6 28.9 1.0
CB B:PRO497 3.7 27.7 1.0
HG2 B:ARG500 3.7 35.8 1.0
N B:ARG500 3.7 27.4 1.0
CB B:PRO385 3.8 37.2 1.0
HB3 B:PRO497 3.8 33.3 1.0
CZ B:ARG500 3.8 33.3 1.0
CE3 B:TRP201 3.8 41.1 1.0
HG2 B:PRO497 3.8 35.3 1.0
CE1 B:TYR202 3.9 34.9 1.0
CZ3 B:TRP201 3.9 37.7 1.0
CG2 B:ILE499 3.9 26.9 1.0
CG B:PRO385 3.9 36.9 1.0
HB3 B:PRO385 3.9 44.7 1.0
CZ B:TYR202 4.0 35.5 1.0
CG B:ARG500 4.0 29.8 1.0
HG23 B:ILE499 4.1 32.3 1.0
HG21 B:ILE499 4.1 32.3 1.0
CA B:ARG500 4.1 27.7 1.0
CD B:ARG500 4.2 32.1 1.0
HA B:ARG500 4.2 33.3 1.0
HH22 B:ARG500 4.3 41.1 1.0
H B:ILE499 4.3 30.7 1.0
HD2 B:PRO385 4.3 46.7 1.0
CG B:PRO497 4.3 29.4 1.0
HB2 B:ARG500 4.3 34.7 1.0
N B:ILE499 4.6 25.5 1.0
HG3 B:PRO385 4.7 44.3 1.0
O B:HOH889 4.7 30.6 1.0
CD B:PRO385 4.7 38.9 1.0
C B:ILE499 4.8 26.6 1.0
HD2 B:ARG500 4.8 38.5 1.0
C B:PRO497 4.8 30.0 1.0
HD3 B:ARG500 4.8 38.5 1.0
CA B:PRO497 4.9 27.8 1.0
HG3 B:PRO497 5.0 35.3 1.0
HG3 B:ARG500 5.0 35.8 1.0
N B:TYR498 5.0 28.9 1.0

Chlorine binding site 4 out of 4 in 6qs1

Go back to Chlorine Binding Sites List in 6qs1
Chlorine binding site 4 out of 4 in the Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Bppb within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl716

b:44.4
occ:1.00
 HZ1 F:LYS8 2.0 52.4 0.9
H B:GLY382 2.4 48.3 1.0
NZ F:LYS8 2.8 43.6 0.9
HA B:PRO385 2.8 43.2 1.0
HZ2 F:LYS8 3.0 52.4 0.9
O B:HOH923 3.0 45.3 1.0
HB3 B:ARG381 3.1 57.6 1.0
HD2 B:HIS388 3.2 47.7 1.0
N B:GLY382 3.2 40.2 1.0
HZ3 F:LYS8 3.4 52.4 0.9
HE3 F:LYS8 3.5 56.4 0.9
HB2 B:HIS388 3.6 43.6 1.0
HA B:ARG381 3.6 53.2 1.0
HG3 B:PRO385 3.6 44.3 1.0
CE F:LYS8 3.6 47.0 0.9
CA B:PRO385 3.7 36.0 1.0
HA3 B:GLY382 3.8 47.0 1.0
CB B:ARG381 3.8 48.0 1.0
CD2 B:HIS388 3.9 39.7 1.0
HE2 F:LYS8 3.9 56.4 0.9
HB3 B:PRO385 4.0 44.7 1.0
HG2 B:ARG381 4.0 60.0 1.0
CA B:ARG381 4.0 44.3 1.0
CA B:GLY382 4.0 39.1 1.0
C B:ARG381 4.1 46.3 1.0
N B:PRO385 4.2 38.9 1.0
CB B:PRO385 4.2 37.2 1.0
HD3 B:ARG381 4.3 79.9 1.0
O B:ASN384 4.3 39.6 1.0
CG B:PRO385 4.3 36.9 1.0
CG B:ARG381 4.3 50.0 1.0
HD2 B:ARG381 4.3 79.9 1.0
CB B:HIS388 4.4 36.3 1.0
C B:ASN384 4.4 43.1 1.0
CG B:HIS388 4.4 34.8 1.0
O B:HOH1020 4.4 51.9 1.0
O F:HOH101 4.5 34.1 1.0
O B:GLY382 4.5 47.3 1.0
CD B:ARG381 4.5 66.6 1.0
HB3 B:HIS388 4.6 43.6 1.0
HB2 B:ARG381 4.6 57.6 1.0
C B:GLY382 4.7 41.1 1.0
CD B:PRO385 4.8 38.9 1.0
C B:PRO385 4.8 32.9 1.0
HA2 B:GLY382 4.9 47.0 1.0
HD3 B:PRO385 4.9 46.7 1.0
O B:PRO385 4.9 34.2 1.0
NE2 B:HIS388 4.9 40.0 1.0
H B:HIS388 4.9 40.2 1.0

Reference:

E.D.Sturrock, L.Lubbe, G.E.Cozier, S.L.U.Schwager, A.T.Arowolo, L.B.Arendse, E.Belcher, K.R.Acharya. Structural Basis For the C-Domain-Selective Angiotensin-Converting Enzyme Inhibition By Bradykinin-Potentiating Peptide B (Bppb). Biochem.J. V. 476 1553 2019.
ISSN: ESSN 1470-8728
PubMed: 31072910
DOI: 10.1042/BCJ20190290
Page generated: Sat Dec 12 13:34:34 2020

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