Chlorine in PDB 6zpt: Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain.

Enzymatic activity of Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain.

All present enzymatic activity of Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain.:
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain., PDB code: 6zpt 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) 69.05 / 2.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 73.650, 99.257, 127.980, 98.63, 89.63, 111.15
R / Rfree (%) 22.4 / 27.8

Other elements in 6zpt:

The structure of Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain. also contains other interesting chemical elements:

Zinc (Zn) 4 atoms
Calcium (Ca) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain. (pdb code 6zpt). 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 the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain., PDB code: 6zpt:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 6zpt

Go back to Chlorine Binding Sites List in 6zpt
Chlorine binding site 1 out of 4 in the Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain.


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 the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl705

b:54.3
occ:1.00
HE A:ARG500 2.0 64.7 1.0
HH A:TYR202 2.4 66.8 1.0
HH21 A:ARG500 2.6 51.7 1.0
HB3 A:ARG500 2.6 62.6 1.0
HB2 A:PRO385 2.8 60.7 1.0
HB2 A:PRO497 2.9 66.4 1.0
NE A:ARG500 2.9 53.9 1.0
OH A:TYR202 3.0 55.7 1.0
HE3 A:TRP201 3.1 69.7 1.0
HZ3 A:TRP201 3.1 68.6 1.0
HB3 A:PRO385 3.1 60.7 1.0
HG2 A:PRO385 3.2 58.5 1.0
HB3 A:PRO497 3.2 66.4 1.0
HG22 A:ILE499 3.2 52.6 1.0
CB A:PRO385 3.3 50.6 1.0
NH2 A:ARG500 3.3 43.1 1.0
H A:ARG500 3.3 59.1 1.0
CB A:PRO497 3.5 55.3 1.0
HE1 A:TYR202 3.5 57.9 1.0
CB A:ARG500 3.5 52.1 1.0
CZ A:ARG500 3.5 57.4 1.0
HG2 A:ARG500 3.6 52.8 1.0
CE3 A:TRP201 3.7 58.0 1.0
CG A:PRO385 3.7 48.7 1.0
CZ3 A:TRP201 3.7 57.2 1.0
HG23 A:ILE499 3.9 52.6 1.0
CG A:ARG500 3.9 44.0 1.0
N A:ARG500 3.9 49.3 1.0
CZ A:TYR202 3.9 51.7 1.0
CD A:ARG500 3.9 49.0 1.0
CG2 A:ILE499 3.9 43.8 1.0
HG2 A:PRO497 4.0 65.4 1.0
CE1 A:TYR202 4.0 48.3 1.0
HH22 A:ARG500 4.1 51.7 1.0
HB2 A:ARG500 4.2 62.6 1.0
CA A:ARG500 4.2 54.5 1.0
HG3 A:PRO385 4.2 58.5 1.0
HG21 A:ILE499 4.3 52.6 1.0
HA A:ARG500 4.3 65.4 1.0
CG A:PRO497 4.3 54.5 1.0
HD3 A:ARG500 4.5 58.8 1.0
HD2 A:ARG500 4.6 58.8 1.0
H A:ILE499 4.7 56.1 1.0
CA A:PRO497 4.7 52.4 1.0
CA A:PRO385 4.7 54.0 1.0
C A:PRO497 4.8 48.7 1.0
HG3 A:PRO497 4.8 65.4 1.0
NH1 A:ARG500 4.8 61.1 1.0
HG3 A:ARG500 4.9 52.8 1.0
HD2 A:PRO385 4.9 55.4 1.0
C A:ILE499 4.9 48.8 1.0
CD A:PRO385 4.9 46.1 1.0
N A:ILE499 4.9 46.8 1.0

Chlorine binding site 2 out of 4 in 6zpt

Go back to Chlorine Binding Sites List in 6zpt
Chlorine binding site 2 out of 4 in the Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain.


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 the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl707

b:60.2
occ:1.00
HE B:ARG500 2.2 65.1 1.0
HH B:TYR202 2.5 60.5 1.0
HB3 B:ARG500 2.6 57.5 1.0
HH21 B:ARG500 2.7 52.1 1.0
HB2 B:PRO385 2.9 71.0 1.0
HB2 B:PRO497 3.0 59.4 1.0
NE B:ARG500 3.0 54.3 1.0
HG22 B:ILE499 3.2 56.4 1.0
HE3 B:TRP201 3.2 48.5 1.0
HG2 B:PRO385 3.2 64.8 1.0
HZ3 B:TRP201 3.2 51.6 1.0
H B:ARG500 3.3 66.2 1.0
OH B:TYR202 3.3 50.5 1.0
NH2 B:ARG500 3.4 43.4 1.0
HE1 B:TYR202 3.4 61.9 1.0
CB B:PRO385 3.5 59.2 1.0
HB3 B:PRO385 3.5 71.0 1.0
HB3 B:PRO497 3.5 59.4 1.0
CB B:ARG500 3.5 47.9 1.0
CZ B:ARG500 3.7 53.5 1.0
CB B:PRO497 3.7 49.5 1.0
HG2 B:ARG500 3.8 55.9 1.0
N B:ARG500 3.8 55.2 1.0
CE3 B:TRP201 3.8 40.4 1.0
CG B:PRO385 3.8 54.0 1.0
CZ3 B:TRP201 3.9 43.0 1.0
HG23 B:ILE499 3.9 56.4 1.0
CG2 B:ILE499 3.9 47.0 1.0
CG B:ARG500 4.0 46.6 1.0
CA B:ARG500 4.1 49.9 1.0
CE1 B:TYR202 4.1 51.6 1.0
CD B:ARG500 4.1 47.4 1.0
HA B:ARG500 4.1 59.9 1.0
CZ B:TYR202 4.1 49.4 1.0
HH22 B:ARG500 4.2 52.1 1.0
HB2 B:ARG500 4.2 57.5 1.0
HG2 B:PRO497 4.2 55.3 1.0
HG21 B:ILE499 4.2 56.4 1.0
HG3 B:PRO385 4.4 64.8 1.0
CG B:PRO497 4.5 46.0 1.0
H B:ILE499 4.6 56.1 1.0
HD3 B:ARG500 4.7 56.9 1.0
HD2 B:PRO385 4.7 57.6 1.0
HD2 B:ARG500 4.7 56.9 1.0
C B:ILE499 4.8 50.3 1.0
C B:PRO497 4.9 51.1 1.0
CD B:PRO385 4.9 48.0 1.0
CA B:PRO497 4.9 51.5 1.0
N B:ILE499 4.9 46.8 1.0
CA B:PRO385 4.9 51.8 1.0
HG3 B:ARG500 5.0 55.9 1.0
NH1 B:ARG500 5.0 56.3 1.0

Chlorine binding site 3 out of 4 in 6zpt

Go back to Chlorine Binding Sites List in 6zpt
Chlorine binding site 3 out of 4 in the Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain.


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 the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl708

b:44.4
occ:1.00
HE C:ARG500 2.1 67.4 1.0
HH C:TYR202 2.5 56.2 1.0
HB3 C:ARG500 2.6 51.8 1.0
HB2 C:PRO497 2.7 66.5 1.0
HH21 C:ARG500 2.8 79.6 1.0
HB2 C:PRO385 3.0 69.5 1.0
NE C:ARG500 3.0 56.2 1.0
H C:ARG500 3.2 54.8 1.0
HG2 C:PRO385 3.2 62.3 1.0
HG22 C:ILE499 3.2 60.8 1.0
HB3 C:PRO497 3.2 66.5 1.0
HZ3 C:TRP201 3.3 74.5 1.0
HE3 C:TRP201 3.3 69.8 1.0
OH C:TYR202 3.3 46.8 1.0
CB C:PRO497 3.4 55.4 1.0
HE1 C:TYR202 3.5 59.9 1.0
NH2 C:ARG500 3.5 66.3 1.0
CB C:ARG500 3.5 43.1 1.0
CB C:PRO385 3.6 58.0 1.0
HB3 C:PRO385 3.6 69.5 1.0
HG2 C:ARG500 3.7 60.5 1.0
CZ C:ARG500 3.7 57.5 1.0
N C:ARG500 3.9 45.6 1.0
CG C:PRO385 3.9 51.9 1.0
CG C:ARG500 3.9 50.5 1.0
CE3 C:TRP201 3.9 58.1 1.0
CZ3 C:TRP201 3.9 62.0 1.0
HG23 C:ILE499 3.9 60.8 1.0
HG2 C:PRO497 4.0 65.5 1.0
CG2 C:ILE499 4.0 50.7 1.0
CD C:ARG500 4.0 59.3 1.0
CE1 C:TYR202 4.1 49.9 1.0
CZ C:TYR202 4.1 46.0 1.0
HB2 C:ARG500 4.2 51.8 1.0
CA C:ARG500 4.2 47.7 1.0
HH22 C:ARG500 4.3 79.6 1.0
CG C:PRO497 4.3 54.6 1.0
HA C:ARG500 4.3 57.2 1.0
HG21 C:ILE499 4.3 60.8 1.0
HG3 C:PRO385 4.4 62.3 1.0
HD3 C:ARG500 4.5 71.2 1.0
C C:PRO497 4.6 54.4 1.0
CA C:PRO497 4.6 52.2 1.0
H C:ILE499 4.6 53.3 1.0
HD2 C:ARG500 4.7 71.2 1.0
HD2 C:PRO385 4.7 65.8 1.0
N C:TYR498 4.8 48.8 1.0
H C:TYR498 4.8 58.6 1.0
O C:PRO497 4.9 53.3 1.0
N C:ILE499 4.9 44.4 1.0
HG3 C:PRO497 4.9 65.5 1.0
HB3 C:TRP198 4.9 70.3 1.0
HG3 C:ARG500 4.9 60.5 1.0
C C:ILE499 4.9 48.0 1.0
CD C:PRO385 4.9 54.8 1.0
CA C:PRO385 5.0 55.9 1.0

Chlorine binding site 4 out of 4 in 6zpt

Go back to Chlorine Binding Sites List in 6zpt
Chlorine binding site 4 out of 4 in the Crystal Structure of the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain.


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 the Open Conformation of S2_S'-Mutant Human Angiotensin-1 Converting Enzyme N-Domain. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl706

b:50.7
occ:1.00
HE D:ARG500 2.4 60.2 1.0
HH D:TYR202 2.6 48.9 1.0
HB3 D:ARG500 2.8 54.6 1.0
HB2 D:PRO497 2.8 58.9 1.0
HH21 D:ARG500 3.0 59.9 1.0
HB2 D:PRO385 3.1 71.3 1.0
HG22 D:ILE499 3.1 41.5 1.0
HB3 D:PRO497 3.1 58.9 1.0
H D:ARG500 3.2 70.0 1.0
NE D:ARG500 3.3 50.2 1.0
OH D:TYR202 3.3 40.7 1.0
CB D:PRO497 3.4 49.1 1.0
HE3 D:TRP201 3.5 78.3 1.0
HG2 D:PRO385 3.5 67.4 1.0
HE1 D:TYR202 3.5 62.8 1.0
HZ3 D:TRP201 3.6 80.1 1.0
CB D:ARG500 3.6 45.5 1.0
NH2 D:ARG500 3.7 49.9 1.0
CB D:PRO385 3.8 59.5 1.0
HG2 D:ARG500 3.8 54.8 1.0
N D:ARG500 3.8 58.4 1.0
HB3 D:PRO385 3.9 71.3 1.0
CG2 D:ILE499 3.9 34.6 1.0
HG23 D:ILE499 3.9 41.5 1.0
CZ D:ARG500 4.0 58.6 1.0
HG2 D:PRO497 4.0 58.1 1.0
CG D:ARG500 4.1 45.7 1.0
CG D:PRO385 4.1 56.1 1.0
CE3 D:TRP201 4.2 65.2 1.0
CA D:ARG500 4.2 43.8 1.0
CE1 D:TYR202 4.2 52.3 1.0
CZ D:TYR202 4.2 46.4 1.0
CZ3 D:TRP201 4.2 66.8 1.0
HA D:ARG500 4.3 52.6 1.0
HG21 D:ILE499 4.3 41.5 1.0
CD D:ARG500 4.3 40.2 1.0
CG D:PRO497 4.3 48.4 1.0
HB2 D:ARG500 4.3 54.6 1.0
H D:ILE499 4.4 59.3 1.0
HH22 D:ARG500 4.5 59.9 1.0
CA D:PRO497 4.6 50.4 1.0
H D:TYR498 4.7 51.8 1.0
C D:PRO497 4.7 44.7 1.0
N D:ILE499 4.7 49.4 1.0
C D:ILE499 4.8 53.8 1.0
HG3 D:PRO385 4.8 67.4 1.0
N D:TYR498 4.8 43.2 1.0
HG3 D:PRO497 4.8 58.1 1.0
HD2 D:PRO385 4.8 58.2 1.0
HD3 D:ARG500 4.8 48.3 1.0
HD2 D:ARG500 4.9 48.3 1.0

Reference:

G.E.Cozier, L.Lubbe, E.D.Sturrock, K.R.Acharya. Angiotensin-Converting Enzyme Open For Business: Structural Insights Into the Sub-Domain Dynamics. Febs J. 2020.
ISSN: ISSN 1742-464X
PubMed: 33067882
DOI: 10.1111/FEBS.15601
Page generated: Sat Dec 12 14:47:54 2020

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