Zinc in PDB 4bzr: Human Testis Angiotensin Converting Enzyme in Complex with K-26

Enzymatic activity of Human Testis Angiotensin Converting Enzyme in Complex with K-26

All present enzymatic activity of Human Testis Angiotensin Converting Enzyme in Complex with K-26:
3.4.15.1;

Protein crystallography data

The structure of Human Testis Angiotensin Converting Enzyme in Complex with K-26, PDB code: 4bzr was solved by G.J.Kramer, A.Mohd, S.L.U.Schwager, G.Masuyer, K.R.Acharya, E.D.Sturrock, B.O.Bachmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.37 / 1.84
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.250, 84.505, 133.481, 90.00, 90.00, 90.00
R / Rfree (%) 21.423 / 25.182

Other elements in 4bzr:

The structure of Human Testis Angiotensin Converting Enzyme in Complex with K-26 also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Testis Angiotensin Converting Enzyme in Complex with K-26 (pdb code 4bzr). 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 Human Testis Angiotensin Converting Enzyme in Complex with K-26, PDB code: 4bzr:

Zinc binding site 1 out of 1 in 4bzr

Go back to Zinc Binding Sites List in 4bzr
Zinc binding site 1 out of 1 in the Human Testis Angiotensin Converting Enzyme in Complex with K-26


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Testis Angiotensin Converting Enzyme in Complex with K-26 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1630

b:18.8
occ:1.00
OE1 A:GLU411 1.9 17.1 1.0
NE2 A:HIS383 2.0 19.8 1.0
NE2 A:HIS387 2.1 17.3 1.0
OAJ A:K261627 2.3 15.5 1.0
OAG A:K261627 2.3 16.4 1.0
PBK A:K261627 2.8 16.2 1.0
CD A:GLU411 2.9 15.9 1.0
CD2 A:HIS383 3.0 18.9 1.0
CE1 A:HIS387 3.0 16.6 1.0
CE1 A:HIS383 3.0 19.4 1.0
CD2 A:HIS387 3.1 16.7 1.0
OE2 A:GLU411 3.2 16.1 1.0
NAY A:K261627 3.9 14.9 1.0
CBI A:K261627 4.0 15.1 1.0
OAK A:K261627 4.1 17.5 1.0
ND1 A:HIS383 4.1 19.6 1.0
CG A:HIS383 4.1 18.4 1.0
ND1 A:HIS387 4.2 16.1 1.0
CG A:HIS387 4.2 16.0 1.0
CE1 A:TYR523 4.3 12.3 1.0
CG A:GLU411 4.3 16.3 1.0
OE2 A:GLU384 4.3 19.7 1.0
O A:HOH2252 4.5 13.6 1.0
C A:K261627 4.5 15.2 1.0
OH A:TYR523 4.5 11.8 1.0
CA A:GLU411 4.5 16.1 1.0
CB A:GLU411 4.6 15.8 1.0
CB A:K261627 4.6 16.0 1.0
O A:HOH2238 4.9 28.8 1.0
CZ A:TYR523 4.9 12.1 1.0
CD A:GLU384 4.9 20.0 1.0
OE1 A:GLU384 5.0 20.3 1.0

Reference:

G.J.Kramer, A.Mohd, S.L.U.Schwager, G.Masuyer, K.R.Acharya, E.D.Sturrock, B.O.Bachmann. Interkingdom Pharmacology of Angiotensin-I Converting Enzyme Inhibitor Phosphonates Produced By Actinomycetes Acs Med.Chem.Lett. V. 5 346 2014.
ISSN: ISSN 1948-5875
PubMed: 24900839
DOI: 10.1021/ML4004588
Page generated: Wed Dec 16 05:07:08 2020

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