Chlorine in PDB 6zpu: Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus.

Enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus.

All present enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus.:
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus., PDB code: 6zpu 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) 53.18 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.453, 84.904, 128.154, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 23.5

Other elements in 6zpu:

The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus. also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus. (pdb code 6zpu). 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 Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus., PDB code: 6zpu:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 6zpu

Go back to Chlorine Binding Sites List in 6zpu
Chlorine binding site 1 out of 2 in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus.


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 Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl717

b:24.6
occ:1.00
HH A:TYR224 2.3 33.9 1.0
HE A:ARG522 2.4 19.8 1.0
HB3 A:ARG522 2.7 21.2 1.0
HB2 A:PRO519 2.8 26.3 1.0
HG22 A:ILE521 2.9 24.9 1.0
HE1 A:TYR224 2.9 27.0 1.0
HH21 A:ARG522 3.0 24.7 1.0
O A:HOH1026 3.0 28.1 1.0
H A:ARG522 3.1 25.9 1.0
OH A:TYR224 3.1 28.2 1.0
HB2 A:PRO407 3.1 27.4 1.0
HG2 A:PRO407 3.2 29.3 1.0
NE A:ARG522 3.2 16.5 1.0
CB A:ARG522 3.5 17.7 1.0
CE1 A:TYR224 3.6 22.5 1.0
CB A:PRO519 3.6 21.9 1.0
HB3 A:PRO519 3.6 26.3 1.0
N A:ARG522 3.6 21.6 1.0
NH2 A:ARG522 3.7 20.6 1.0
CG2 A:ILE521 3.7 20.8 1.0
HG2 A:ARG522 3.7 22.5 1.0
HG23 A:ILE521 3.7 24.9 1.0
CZ A:TYR224 3.8 21.6 1.0
CB A:PRO407 3.8 22.9 1.0
HB3 A:PRO407 3.8 27.4 1.0
CG A:PRO407 3.9 24.4 1.0
CZ A:ARG522 3.9 23.4 1.0
CA A:ARG522 4.0 19.3 1.0
CG A:ARG522 4.0 18.8 1.0
HA A:ARG522 4.0 23.1 1.0
HG21 A:ILE521 4.1 24.9 1.0
HG2 A:PRO519 4.1 33.2 1.0
CD A:ARG522 4.2 19.8 1.0
HB2 A:ARG522 4.2 21.2 1.0
H A:ILE521 4.4 27.7 1.0
CG A:PRO519 4.4 27.6 1.0
SD A:MET223 4.4 31.5 1.0
HH22 A:ARG522 4.5 24.7 1.0
HG3 A:PRO407 4.5 29.3 1.0
HB2 A:MET223 4.6 23.8 1.0
C A:ILE521 4.6 24.3 1.0
C A:PRO519 4.7 26.1 1.0
N A:ILE521 4.7 23.1 1.0
HD2 A:PRO407 4.7 28.0 1.0
CA A:PRO519 4.8 23.2 1.0
HD3 A:ARG522 4.8 23.7 1.0
CD1 A:TYR224 4.8 27.0 1.0
O A:PRO519 4.8 20.6 1.0
HD2 A:ARG522 4.8 23.7 1.0
O A:HOH895 4.9 20.8 1.0
CD A:PRO407 4.9 23.4 1.0
N A:TYR520 4.9 22.2 1.0
CB A:ILE521 4.9 22.6 1.0
HG3 A:ARG522 4.9 22.5 1.0
HB3 A:TRP220 5.0 28.6 1.0
CA A:ILE521 5.0 23.3 1.0

Chlorine binding site 2 out of 2 in 6zpu

Go back to Chlorine Binding Sites List in 6zpu
Chlorine binding site 2 out of 2 in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus.


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 Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl718

b:28.3
occ:1.00
HH11 A:ARG186 2.2 29.2 1.0
HE A:ARG186 2.3 30.4 1.0
HE1 A:TRP485 2.6 31.7 1.0
HH11 A:ARG489 2.7 32.0 1.0
HB3 A:ASP507 2.9 32.4 1.0
NH1 A:ARG186 3.0 24.4 1.0
NE A:ARG186 3.1 25.3 1.0
O A:HOH860 3.2 27.2 1.0
NH1 A:ARG489 3.2 26.7 1.0
HZ2 A:TRP486 3.3 32.1 1.0
HE A:ARG489 3.4 22.4 1.0
NE1 A:TRP485 3.5 26.4 1.0
CZ A:ARG186 3.5 18.3 1.0
CZ2 A:TRP486 3.6 26.8 1.0
HH12 A:ARG489 3.6 32.0 1.0
HH12 A:ARG186 3.7 29.2 1.0
HZ2 A:TRP485 3.8 33.2 1.0
CB A:ASP507 3.8 27.0 1.0
HZ2 A:TRP182 3.8 22.7 1.0
CZ A:ARG489 3.8 21.9 1.0
NE A:ARG489 3.8 18.7 1.0
HH2 A:TRP486 3.9 33.7 1.0
HB2 A:ASP507 4.0 32.4 1.0
CH2 A:TRP486 4.0 28.1 1.0
HD1 A:TRP279 4.2 27.4 1.0
CE2 A:TRP485 4.3 26.3 1.0
HD3 A:ARG186 4.3 33.5 1.0
CD A:ARG186 4.3 27.9 1.0
CZ2 A:TRP485 4.4 27.6 1.0
CE2 A:TRP486 4.4 28.8 1.0
CZ2 A:TRP182 4.4 18.9 1.0
HE1 A:TRP182 4.5 25.5 1.0
O A:ASP507 4.5 24.3 1.0
CD1 A:TRP485 4.5 27.6 1.0
CG A:ASP507 4.5 27.0 1.0
HD1 A:TRP485 4.6 33.1 1.0
HG2 A:ARG186 4.7 33.0 1.0
C A:ASP507 4.8 25.4 1.0
HA A:TRP279 4.8 25.0 1.0
CA A:ASP507 4.8 25.2 1.0
HE1 A:TRP486 4.8 37.0 1.0
NH2 A:ARG186 4.8 25.2 1.0
O A:HOH919 4.9 23.3 1.0
NH2 A:ARG489 4.9 18.0 1.0
OD2 A:ASP507 4.9 26.2 1.0
HG3 A:ARG489 4.9 31.9 1.0
NE1 A:TRP182 4.9 21.2 1.0
NE1 A:TRP486 4.9 30.8 1.0
HD3 A:ARG489 5.0 21.0 1.0
CD A:ARG489 5.0 17.5 1.0
HA A:ASP507 5.0 30.3 1.0
CE2 A:TRP182 5.0 18.2 1.0
CZ3 A:TRP486 5.0 24.1 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 14:48:01 2020

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