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Chlorine in PDB 1uze: Complex of the Anti-Hypertensive Drug Enalaprilat and the Human Testicular Angiotensin I-Converting Enzyme

Protein crystallography data

The structure of Complex of the Anti-Hypertensive Drug Enalaprilat and the Human Testicular Angiotensin I-Converting Enzyme, PDB code: 1uze was solved by R.Natesh, S.L.U.Schwager, H.R.Evans, 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) 50 / 1.82
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.720, 85.350, 133.730, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 21.1

Other elements in 1uze:

The structure of Complex of the Anti-Hypertensive Drug Enalaprilat and the Human Testicular Angiotensin I-Converting Enzyme also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Complex of the Anti-Hypertensive Drug Enalaprilat and the Human Testicular Angiotensin I-Converting Enzyme (pdb code 1uze). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Complex of the Anti-Hypertensive Drug Enalaprilat and the Human Testicular Angiotensin I-Converting Enzyme, PDB code: 1uze:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1uze

Go back to Chlorine Binding Sites List in 1uze
Chlorine binding site 1 out of 2 in the Complex of the Anti-Hypertensive Drug Enalaprilat and the Human Testicular Angiotensin I-Converting Enzyme


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Complex of the Anti-Hypertensive Drug Enalaprilat and the Human Testicular Angiotensin I-Converting Enzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl703

b:14.8
occ:1.00
NE A:ARG186 3.1 13.8 1.0
O A:HOH2375 3.2 16.3 1.0
NH1 A:ARG489 3.2 12.5 1.0
NH1 A:ARG186 3.3 13.9 1.0
NE1 A:TRP485 3.3 13.0 1.0
CZ2 A:TRP486 3.5 11.7 1.0
CZ A:ARG186 3.7 15.8 1.0
CZ A:ARG489 3.8 12.4 1.0
CB A:ASP507 3.8 12.8 1.0
NE A:ARG489 3.8 11.9 1.0
CH2 A:TRP486 4.0 12.7 1.0
CE2 A:TRP485 4.1 12.5 1.0
CD A:ARG186 4.3 16.5 1.0
CD1 A:TRP485 4.3 12.1 1.0
CZ2 A:TRP485 4.3 13.1 1.0
CE2 A:TRP486 4.4 11.2 1.0
CZ2 A:TRP182 4.4 12.1 1.0
O A:ASP507 4.5 13.4 1.0
CG A:ASP507 4.5 14.0 1.0
C A:ASP507 4.7 12.5 1.0
NE1 A:TRP486 4.8 12.2 1.0
CA A:ASP507 4.8 12.1 1.0
O A:HOH2240 4.8 12.3 1.0
NH2 A:ARG489 4.8 11.3 1.0
OD2 A:ASP507 4.9 16.4 1.0
CD A:ARG489 4.9 12.5 1.0
NH2 A:ARG186 5.0 15.5 1.0

Chlorine binding site 2 out of 2 in 1uze

Go back to Chlorine Binding Sites List in 1uze
Chlorine binding site 2 out of 2 in the Complex of the Anti-Hypertensive Drug Enalaprilat and the Human Testicular Angiotensin I-Converting Enzyme


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Complex of the Anti-Hypertensive Drug Enalaprilat and the Human Testicular Angiotensin I-Converting Enzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl704

b:14.3
occ:1.00
O A:HOH2172 3.1 14.3 1.0
OH A:TYR224 3.1 11.0 1.0
NE A:ARG522 3.1 12.2 1.0
CB A:ARG522 3.5 8.8 1.0
NH2 A:ARG522 3.5 12.2 1.0
CB A:PRO519 3.6 10.1 1.0
N A:ARG522 3.6 10.1 1.0
CB A:PRO407 3.6 12.4 1.0
CG2 A:ILE521 3.7 13.0 1.0
CE1 A:TYR224 3.7 10.8 1.0
CZ A:ARG522 3.8 12.3 1.0
CZ A:TYR224 3.8 10.2 1.0
CG A:PRO407 3.9 14.7 1.0
CA A:ARG522 4.0 9.8 1.0
CE A:MET223 4.0 18.0 1.0
CG A:ARG522 4.0 9.2 1.0
CD A:ARG522 4.2 11.8 1.0
C A:ILE521 4.6 9.9 1.0
CG A:PRO519 4.6 10.2 1.0
N A:ILE521 4.6 9.3 1.0
C A:PRO519 4.7 12.8 1.0
CA A:PRO519 4.7 10.5 1.0
O A:PRO519 4.8 13.1 1.0
O A:HOH2339 4.8 12.0 1.0
CD A:PRO407 4.9 11.9 1.0
CB A:ILE521 4.9 11.8 1.0
CA A:ILE521 4.9 9.9 1.0
N A:TYR520 4.9 11.4 1.0
CD1 A:TYR224 5.0 10.8 1.0

Reference:

R.Natesh, S.L.U.Schwager, H.R.Evans, E.D.Sturrock, K.R.Acharya. Structural Details on the Binding of Antihypertensive Drugs Captopril and Enalaprilat to Human Testicular Angiotensin I-Converting Enzyme Biochemistry V. 43 8718 2004.
ISSN: ISSN 0006-2960
PubMed: 15236580
DOI: 10.1021/BI049480N
Page generated: Sat Dec 12 08:51:21 2020

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