Chlorine in PDB 4ufb: Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro

Enzymatic activity of Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro

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

Protein crystallography data

The structure of Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro, PDB code: 4ufb was solved by G.Masuyer, R.G.Douglas, E.D.Sturrock, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 113.94 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 73.480, 101.590, 114.510, 85.46, 85.90, 81.62
R / Rfree (%) 20.7 / 23.5

Other elements in 4ufb:

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

Zinc (Zn) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro (pdb code 4ufb). 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 Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro, PDB code: 4ufb:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 4ufb

Go back to Chlorine Binding Sites List in 4ufb
Chlorine binding site 1 out of 4 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro


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 Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1002

b:22.0
occ:1.00
 O A:HOH2169 3.0 25.9 1.0
OH A:TYR202 3.1 24.2 1.0
NE A:ARG500 3.2 20.6 1.0
NH2 A:ARG500 3.5 21.1 1.0
CB A:ARG500 3.6 20.3 1.0
CB A:PRO385 3.6 23.3 1.0
N A:ARG500 3.6 20.5 1.0
CB A:PRO497 3.7 20.2 1.0
CE1 A:TYR202 3.8 24.9 1.0
CG A:PRO385 3.8 23.3 1.0
CG2 A:ILE499 3.8 21.1 1.0
CZ A:ARG500 3.8 21.0 1.0
CE3 A:TRP201 3.9 30.4 1.0
CZ A:TYR202 3.9 25.2 1.0
CZ3 A:TRP201 3.9 30.8 1.0
CA A:ARG500 4.0 20.1 1.0
CG A:ARG500 4.1 20.4 1.0
CD A:ARG500 4.3 20.9 1.0
CG A:PRO497 4.6 21.1 1.0
N A:ILE499 4.6 20.7 1.0
CD A:PRO385 4.6 23.4 1.0
C A:ILE499 4.6 20.6 1.0
C A:PRO497 4.7 20.4 1.0
CA A:PRO497 4.8 20.0 1.0
O A:HOH2293 4.9 24.8 1.0
N A:TYR498 4.9 20.3 1.0
OD2 A:ASP443 4.9 27.7 1.0
CA A:ILE499 4.9 20.4 1.0
O A:PRO497 5.0 19.9 1.0
CB A:ILE499 5.0 20.8 1.0

Chlorine binding site 2 out of 4 in 4ufb

Go back to Chlorine Binding Sites List in 4ufb
Chlorine binding site 2 out of 4 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro


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 Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1002

b:22.5
occ:1.00
 O B:HOH2151 3.0 21.1 1.0
OH B:TYR202 3.0 23.3 1.0
NE B:ARG500 3.3 18.1 1.0
CB B:ARG500 3.6 18.8 1.0
NH2 B:ARG500 3.6 18.0 1.0
CE1 B:TYR202 3.6 24.8 1.0
CB B:PRO385 3.7 22.2 1.0
CB B:PRO497 3.7 18.7 1.0
N B:ARG500 3.7 19.5 1.0
CZ B:TYR202 3.8 25.0 1.0
CG B:PRO385 3.9 22.2 1.0
CG2 B:ILE499 3.9 19.3 1.0
CE3 B:TRP201 3.9 30.9 1.0
CZ B:ARG500 3.9 18.2 1.0
CZ3 B:TRP201 3.9 30.1 1.0
CA B:ARG500 4.0 19.3 1.0
CG B:ARG500 4.1 18.4 1.0
CD B:ARG500 4.3 18.4 1.0
CG B:PRO497 4.6 19.0 1.0
C B:ILE499 4.6 19.4 1.0
N B:ILE499 4.6 18.9 1.0
CD B:PRO385 4.7 23.0 1.0
C B:PRO497 4.8 18.4 1.0
O B:HOH2286 4.8 22.7 1.0
CA B:PRO497 4.8 18.4 1.0
CD1 B:TYR202 4.9 25.8 1.0
CA B:ILE499 5.0 19.1 1.0
N B:TYR498 5.0 18.3 1.0
O B:PRO497 5.0 17.7 1.0

Chlorine binding site 3 out of 4 in 4ufb

Go back to Chlorine Binding Sites List in 4ufb
Chlorine binding site 3 out of 4 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro


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 Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cl1002

b:18.9
occ:1.00
 OH C:TYR202 3.1 20.5 1.0
O C:HOH2174 3.1 18.7 1.0
NE C:ARG500 3.2 16.2 1.0
NH2 C:ARG500 3.5 16.1 1.0
CB C:ARG500 3.6 16.8 1.0
CB C:PRO385 3.6 18.8 1.0
CB C:PRO497 3.7 18.2 1.0
N C:ARG500 3.7 17.3 1.0
CE2 C:TYR202 3.8 22.1 1.0
CG C:PRO385 3.8 18.9 1.0
CE3 C:TRP201 3.8 26.2 1.0
CZ C:ARG500 3.8 16.3 1.0
CZ3 C:TRP201 3.9 25.7 1.0
CZ C:TYR202 3.9 21.6 1.0
CG2 C:ILE499 3.9 17.9 1.0
CG C:ARG500 4.0 16.7 1.0
CA C:ARG500 4.1 17.1 1.0
CD C:ARG500 4.2 16.4 1.0
CG C:PRO497 4.6 18.4 1.0
CD C:PRO385 4.6 19.6 1.0
N C:ILE499 4.7 17.2 1.0
C C:ILE499 4.7 17.6 1.0
C C:PRO497 4.7 18.0 1.0
CA C:PRO497 4.8 18.0 1.0
O C:HOH2337 4.9 20.5 1.0
N C:TYR498 4.9 17.7 1.0

Chlorine binding site 4 out of 4 in 4ufb

Go back to Chlorine Binding Sites List in 4ufb
Chlorine binding site 4 out of 4 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro


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 Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cl1002

b:20.1
occ:1.00
 O D:HOH2170 3.1 18.6 1.0
OH D:TYR202 3.1 20.1 1.0
NE D:ARG500 3.2 15.5 1.0
CB D:ARG500 3.5 15.7 1.0
NH2 D:ARG500 3.6 15.7 1.0
CB D:PRO385 3.6 18.1 1.0
N D:ARG500 3.7 15.6 1.0
CB D:PRO497 3.7 18.2 1.0
CE2 D:TYR202 3.7 21.1 1.0
CG D:PRO385 3.8 18.2 1.0
CZ D:TYR202 3.8 20.9 1.0
CZ D:ARG500 3.8 16.1 1.0
CG2 D:ILE499 3.9 16.1 1.0
CE3 D:TRP201 3.9 28.6 1.0
CZ3 D:TRP201 4.0 29.1 1.0
CG D:ARG500 4.0 15.4 1.0
CA D:ARG500 4.0 15.6 1.0
CD D:ARG500 4.2 15.8 1.0
CG D:PRO497 4.6 18.4 1.0
CD D:PRO385 4.7 18.2 1.0
C D:ILE499 4.7 15.8 1.0
N D:ILE499 4.7 16.0 1.0
C D:PRO497 4.7 17.9 1.0
CA D:PRO497 4.9 18.1 1.0
O D:HOH2341 4.9 22.9 1.0
O D:PRO497 4.9 18.0 1.0
CD2 D:TYR202 5.0 21.6 1.0

Reference:

G.Masuyer, R.G.Douglas, E.D.Sturrock, K.R.Acharya. Structural Basis of Ac-Sdkp Hydrolysis By Angiotensin-I Converting Enzyme Sci.Rep. V. 5 13742 2015.
ISSN: ESSN 2045-2322
PubMed: 26403559
DOI: 10.1038/SREP13742
Page generated: Sat Dec 12 11:15:08 2020

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