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Zinc in PDB 6f9u: Crystal Structure of Human Testis Angiotensin-1 Converting Enzyme in Complex with Sampatrilat-Asp.

Enzymatic activity of Crystal Structure of Human Testis Angiotensin-1 Converting Enzyme in Complex with Sampatrilat-Asp.

All present enzymatic activity of Crystal Structure of Human Testis Angiotensin-1 Converting Enzyme in Complex with Sampatrilat-Asp.:
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of Human Testis Angiotensin-1 Converting Enzyme in Complex with Sampatrilat-Asp., PDB code: 6f9u was solved by G.E.Cozier, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 72.17 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 56.316, 85.861, 133.233, 90.00, 90.00, 90.00
R / Rfree (%) 16.7 / 20.9

Other elements in 6f9u:

The structure of Crystal Structure of Human Testis Angiotensin-1 Converting Enzyme in Complex with Sampatrilat-Asp. 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 Testis Angiotensin-1 Converting Enzyme in Complex with Sampatrilat-Asp. (pdb code 6f9u). 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 Testis Angiotensin-1 Converting Enzyme in Complex with Sampatrilat-Asp., PDB code: 6f9u:

Zinc binding site 1 out of 1 in 6f9u

Go back to Zinc Binding Sites List in 6f9u
Zinc binding site 1 out of 1 in the Crystal Structure of Human Testis Angiotensin-1 Converting Enzyme in Complex with Sampatrilat-Asp.


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 Testis Angiotensin-1 Converting Enzyme in Complex with Sampatrilat-Asp. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn707

b:21.1
occ:1.00
 OE1 A:GLU411 2.0 18.4 1.0
NE2 A:HIS387 2.0 19.4 1.0
NE2 A:HIS383 2.0 21.6 1.0
O37 A:D0W711 2.1 22.1 1.0
O38 A:D0W711 2.6 21.9 1.0
C36 A:D0W711 2.6 23.8 1.0
CD A:GLU411 2.9 19.6 1.0
CE1 A:HIS387 2.9 24.2 1.0
CE1 A:HIS383 3.0 24.6 1.0
CD2 A:HIS387 3.0 22.2 1.0
HE1 A:HIS387 3.0 29.0 1.0
CD2 A:HIS383 3.1 19.7 1.0
OE2 A:GLU411 3.1 20.9 1.0
HE1 A:HIS383 3.1 29.5 1.0
HD2 A:HIS387 3.3 26.6 1.0
HD2 A:HIS383 3.3 23.6 1.0
HE1 A:TYR523 3.3 22.8 1.0
H061 A:D0W711 3.4 75.9 1.0
H201 A:D0W711 3.5 28.3 1.0
HH A:TYR523 3.6 25.0 1.0
HA A:GLU411 3.7 25.7 1.0
H202 A:D0W711 3.9 28.3 1.0
ND1 A:HIS387 4.0 26.4 1.0
ND1 A:HIS383 4.1 18.3 1.0
CG A:HIS387 4.1 21.1 1.0
C14 A:D0W711 4.1 21.7 1.0
C20 A:D0W711 4.2 23.6 1.0
CG A:HIS383 4.2 19.5 1.0
CE1 A:TYR523 4.2 19.0 1.0
CG A:GLU411 4.3 22.8 1.0
C06 A:D0W711 4.3 63.2 1.0
HB3 A:GLU411 4.4 24.4 1.0
OH A:TYR523 4.4 20.8 1.0
H141 A:D0W711 4.5 26.0 1.0
CA A:GLU411 4.5 21.4 1.0
H062 A:D0W711 4.5 75.9 1.0
CB A:GLU411 4.6 20.3 1.0
N12 A:D0W711 4.7 33.3 1.0
OE2 A:GLU384 4.7 26.6 1.0
HG3 A:GLU411 4.7 27.3 1.0
C10 A:D0W711 4.8 32.6 1.0
HD1 A:HIS387 4.8 31.7 1.0
H121 A:D0W711 4.8 40.0 1.0
HG2 A:GLU411 4.8 27.3 1.0
CZ A:TYR523 4.8 19.0 1.0
HD1 A:HIS383 4.9 22.0 1.0
H151 A:D0W711 4.9 34.2 1.0
C15 A:D0W711 4.9 28.5 1.0
C13 A:D0W711 4.9 28.6 1.0
C16 A:D0W711 5.0 24.2 1.0
O11 A:D0W711 5.0 36.4 1.0

Reference:

G.E.Cozier, S.L.Schwager, R.K.Sharma, K.Chibale, E.D.Sturrock, K.R.Acharya. Crystal Structures of Sampatrilat and Sampatrilat-Asp in Complex with Human Ace - A Molecular Basis For Domain Selectivity. Febs J. V. 285 1477 2018.
ISSN: ISSN 1742-4658
PubMed: 29476645
DOI: 10.1111/FEBS.14421
Page generated: Mon Oct 28 20:48:15 2024

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