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Zinc in PDB 3l3n: Testis Ace Co-Crystal Structure with Novel Inhibitor Lisw

Enzymatic activity of Testis Ace Co-Crystal Structure with Novel Inhibitor Lisw

All present enzymatic activity of Testis Ace Co-Crystal Structure with Novel Inhibitor Lisw:
3.4.15.1;

Protein crystallography data

The structure of Testis Ace Co-Crystal Structure with Novel Inhibitor Lisw, PDB code: 3l3n was solved by J.M.Watermeyer, W.L.Kroger, H.G.O'neil, B.T.Sewell, E.D.Sturrock, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 43.00 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.383, 84.789, 133.958, 90.00, 90.00, 90.00
R / Rfree (%) 22.6 / 26.6

Other elements in 3l3n:

The structure of Testis Ace Co-Crystal Structure with Novel Inhibitor Lisw also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Testis Ace Co-Crystal Structure with Novel Inhibitor Lisw (pdb code 3l3n). 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 Testis Ace Co-Crystal Structure with Novel Inhibitor Lisw, PDB code: 3l3n:

Zinc binding site 1 out of 1 in 3l3n

Go back to Zinc Binding Sites List in 3l3n
Zinc binding site 1 out of 1 in the Testis Ace Co-Crystal Structure with Novel Inhibitor Lisw


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Testis Ace Co-Crystal Structure with Novel Inhibitor Lisw within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:19.6
occ:1.00
OE1 A:GLU411 1.9 23.0 1.0
NE2 A:HIS387 2.1 20.3 1.0
NE2 A:HIS383 2.1 21.4 1.0
O A:LSW1 2.2 21.6 1.0
OXT A:LSW1 2.4 22.6 1.0
C A:LSW1 2.6 23.1 1.0
CD A:GLU411 2.9 23.8 1.0
CE1 A:HIS387 2.9 22.7 1.0
CE1 A:HIS383 3.0 21.0 1.0
CD2 A:HIS383 3.1 20.5 1.0
OE2 A:GLU411 3.1 23.8 1.0
CD2 A:HIS387 3.2 21.6 1.0
CA A:LSW1 4.1 23.7 1.0
ND1 A:HIS387 4.1 23.5 1.0
ND1 A:HIS383 4.1 21.0 1.0
CE2 A:TYR523 4.2 21.7 1.0
CG A:HIS383 4.2 20.1 1.0
CG A:GLU411 4.2 21.1 1.0
CG A:HIS387 4.2 21.3 1.0
OH A:TYR523 4.4 24.1 1.0
CBI A:LSW1 4.4 25.1 1.0
CA A:GLU411 4.5 23.1 1.0
O A:HOH1041 4.5 22.2 1.0
OE2 A:GLU384 4.5 21.6 1.0
O A:HOH1109 4.5 26.8 1.0
CB A:GLU411 4.6 22.6 1.0
N A:LSW1 4.7 23.4 1.0
CZ A:TYR523 4.8 21.7 1.0

Reference:

J.M.Watermeyer, W.L.Kroger, H.G.O'neill, B.T.Sewell, E.D.Sturrock. Characterization of Domain-Selective Inhibitor Binding in Angiotensin-Converting Enzyme Using A Novel Derivative of Lisinopril. Biochem.J. V. 428 67 2010.
ISSN: ISSN 0264-6021
PubMed: 20233165
DOI: 10.1042/BJ20100056
Page generated: Wed Dec 16 04:31:46 2020

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