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Zinc 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:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the Complex of the Anti-Hypertensive Drug Enalaprilat and the Human Testicular Angiotensin I-Converting Enzyme, PDB code: 1uze:

Zinc binding site 1 out of 1 in 1uze

Go back to Zinc Binding Sites List in 1uze
Zinc binding site 1 out of 1 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 Zinc with other atoms in the Zn 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:Zn701

b:15.3
occ:1.00
OE1 A:GLU411 1.9 10.8 1.0
O3 A:EAL3002 2.0 14.7 1.0
NE2 A:HIS387 2.0 14.4 1.0
NE2 A:HIS383 2.1 16.0 1.0
C3 A:EAL3002 2.7 15.6 1.0
O2 A:EAL3002 2.7 16.6 1.0
CD A:GLU411 2.8 11.6 1.0
CE1 A:HIS387 3.0 15.9 1.0
OE2 A:GLU411 3.0 13.2 1.0
CE1 A:HIS383 3.0 14.6 1.0
CD2 A:HIS383 3.1 14.1 1.0
CD2 A:HIS387 3.1 15.5 1.0
ND1 A:HIS387 4.1 14.6 1.0
C4 A:EAL3002 4.1 17.8 1.0
ND1 A:HIS383 4.1 13.3 1.0
CE2 A:TYR523 4.1 9.2 1.0
CG A:GLU411 4.2 10.1 1.0
CG A:HIS383 4.2 15.1 1.0
CG A:HIS387 4.2 15.6 1.0
OH A:TYR523 4.4 10.3 1.0
O A:HOH2320 4.4 17.3 1.0
CA A:GLU411 4.5 12.7 1.0
O A:HOH2281 4.5 20.1 1.0
CB A:GLU411 4.6 13.4 1.0
N1 A:EAL3002 4.6 18.8 1.0
OE2 A:GLU384 4.6 15.1 1.0
C2 A:EAL3002 4.6 16.9 1.0
CZ A:TYR523 4.8 9.3 1.0
C14 A:EAL3002 4.8 20.4 1.0
O A:HOH2111 4.9 40.6 1.0
OE1 A:GLU384 5.0 15.4 1.0
C8 A:EAL3002 5.0 16.3 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: Wed Oct 16 19:40:27 2024

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