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Zinc in PDB 1o86: Crystal Structure of Human Angiotensin Converting Enzyme in Complex with Lisinopril.

Enzymatic activity of Crystal Structure of Human Angiotensin Converting Enzyme in Complex with Lisinopril.

All present enzymatic activity of Crystal Structure of Human Angiotensin Converting Enzyme in Complex with Lisinopril.:
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of Human Angiotensin Converting Enzyme in Complex with Lisinopril., PDB code: 1o86 was solved by R.Natesh, S.L.U.Schwager, 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) 47.14 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.470, 84.900, 133.990, 90.00, 90.00, 90.00
R / Rfree (%) 18 / 22

Other elements in 1o86:

The structure of Crystal Structure of Human Angiotensin Converting Enzyme in Complex with Lisinopril. also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human Angiotensin Converting Enzyme in Complex with Lisinopril. (pdb code 1o86). 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 Crystal Structure of Human Angiotensin Converting Enzyme in Complex with Lisinopril., PDB code: 1o86:

Zinc binding site 1 out of 1 in 1o86

Go back to Zinc Binding Sites List in 1o86
Zinc binding site 1 out of 1 in the Crystal Structure of Human Angiotensin Converting Enzyme in Complex with Lisinopril.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human Angiotensin Converting Enzyme in Complex with Lisinopril. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:25.1
occ:1.00
 OE1 A:GLU411 2.0 9.0 1.0
NE2 A:HIS383 2.0 12.1 1.0
NE2 A:HIS387 2.1 12.8 1.0
O3 A:LPR702 2.1 13.9 1.0
O2 A:LPR702 2.6 15.2 1.0
C3 A:LPR702 2.7 13.6 1.0
CD A:GLU411 2.9 8.6 1.0
CE1 A:HIS387 2.9 11.5 1.0
CE1 A:HIS383 3.0 14.7 1.0
CD2 A:HIS383 3.0 13.2 1.0
OE2 A:GLU411 3.1 8.5 1.0
CD2 A:HIS387 3.2 9.7 1.0
ND1 A:HIS383 4.1 14.3 1.0
ND1 A:HIS387 4.1 13.1 1.0
CG A:HIS383 4.1 15.4 1.0
C4 A:LPR702 4.2 14.8 1.0
CE2 A:TYR523 4.2 8.9 1.0
CG A:HIS387 4.2 12.6 1.0
CG A:GLU411 4.3 7.9 1.0
O A:HOH2409 4.4 12.8 1.0
OH A:TYR523 4.4 8.4 1.0
CA A:GLU411 4.5 10.7 1.0
O A:HOH2570 4.5 16.6 1.0
OE2 A:GLU384 4.6 12.5 1.0
CB A:GLU411 4.6 11.1 1.0
C2 A:LPR702 4.6 12.8 1.0
N1 A:LPR702 4.6 14.8 1.0
CZ A:TYR523 4.8 10.4 1.0
O A:HOH2179 4.8 37.7 1.0
C14 A:LPR702 4.9 12.0 1.0
C8 A:LPR702 5.0 12.5 1.0
OE1 A:GLU384 5.0 11.5 1.0

Reference:

R.Natesh, S.L.U.Schwager, E.D.Sturrock, K.R.Acharya. Crystal Structure of the Human Angiotensin-Converting Enzyme-Lisinopril Complex Nature V. 421 551 2003.
ISSN: ISSN 0028-0836
PubMed: 12540854
DOI: 10.1038/NATURE01370
Page generated: Wed Oct 16 17:28:18 2024

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