Atomistry » Zinc » PDB 6tm9-6ty2 » 6tt4
Atomistry »
  Zinc »
    PDB 6tm9-6ty2 »
      6tt4 »

Zinc in PDB 6tt4: Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.

Enzymatic activity of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.

All present enzymatic activity of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.:
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat., PDB code: 6tt4 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) 64.01 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 74.371, 78.825, 89.686, 92.43, 105.97, 114.60
R / Rfree (%) 18.2 / 22.2

Other elements in 6tt4:

The structure of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat. also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat. (pdb code 6tt4). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat., PDB code: 6tt4:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 6tt4

Go back to Zinc Binding Sites List in 6tt4
Zinc binding site 1 out of 2 in the Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.


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 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn708

b:27.9
occ:1.00
 OE2 A:GLU389 2.0 26.1 1.0
NE2 A:HIS365 2.1 27.7 1.0
NE2 A:HIS361 2.1 28.4 1.0
S2 A:FT8709 2.5 30.9 1.0
O4 A:FT8709 2.5 28.0 1.0
CD A:GLU389 2.9 26.6 1.0
CE1 A:HIS365 3.0 27.5 1.0
CE1 A:HIS361 3.0 28.9 1.0
C11 A:FT8709 3.0 31.1 1.0
CD2 A:HIS361 3.1 26.7 1.0
CD2 A:HIS365 3.1 26.9 1.0
HE1 A:HIS365 3.2 33.0 1.0
OE1 A:GLU389 3.2 26.0 1.0
HE1 A:HIS361 3.2 34.7 1.0
HD2 A:HIS361 3.3 32.1 1.0
HD2 A:HIS365 3.3 32.2 1.0
C12 A:FT8709 3.5 32.4 1.0
HE1 A:TYR501 3.6 32.6 1.0
HH A:TYR501 3.7 32.9 1.0
HA A:GLU389 3.8 32.5 1.0
N2 A:FT8709 4.0 26.7 1.0
ND1 A:HIS361 4.1 28.1 1.0
ND1 A:HIS365 4.1 28.2 1.0
H51 A:BCN716 4.2 50.6 0.8
CG A:HIS361 4.2 25.2 1.0
C13 A:FT8709 4.2 33.6 1.0
CG A:HIS365 4.2 27.1 1.0
H62 A:BCN716 4.3 48.5 0.8
OE2 A:GLU362 4.3 25.9 1.0
CG A:GLU389 4.3 27.2 1.0
C3 A:FT8709 4.4 29.2 1.0
H52 A:BCN716 4.4 50.6 0.8
OH A:TYR501 4.5 27.4 1.0
CE1 A:TYR501 4.5 27.1 1.0
HB3 A:GLU389 4.6 31.7 1.0
C5 A:BCN716 4.6 42.2 0.8
CA A:GLU389 4.7 27.1 1.0
HG3 A:GLU389 4.7 32.6 1.0
O A:HOH991 4.7 29.2 1.0
CB A:GLU389 4.8 26.4 1.0
OE1 A:GLU362 4.8 27.5 1.0
CD A:GLU362 4.8 26.0 1.0
C6 A:BCN716 4.8 40.4 0.8
H61 A:BCN716 4.9 48.5 0.8
HD1 A:HIS361 4.9 33.8 1.0
HG2 A:GLU389 4.9 32.6 1.0
HD1 A:HIS365 4.9 33.8 1.0
HA A:GLU362 5.0 28.6 1.0
CZ A:TYR501 5.0 27.4 1.0

Zinc binding site 2 out of 2 in 6tt4

Go back to Zinc Binding Sites List in 6tt4
Zinc binding site 2 out of 2 in the Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of 'RES_S2 Mutant Human Angiotensin-1 Converting Enzyme N-Domain in Complex with Omapatrilat. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn710

b:26.3
occ:1.00
 OE1 B:GLU389 2.0 27.1 1.0
NE2 B:HIS361 2.1 24.9 1.0
NE2 B:HIS365 2.1 27.5 1.0
S2 B:FT8711 2.5 31.0 1.0
O4 B:FT8711 2.6 23.1 1.0
CD B:GLU389 3.0 26.6 1.0
CD2 B:HIS361 3.1 24.9 1.0
C11 B:FT8711 3.1 28.7 1.0
CE1 B:HIS361 3.1 26.8 1.0
CE1 B:HIS365 3.1 26.7 1.0
CD2 B:HIS365 3.1 26.7 1.0
HD2 B:HIS361 3.2 29.9 1.0
HE1 B:HIS365 3.2 32.1 1.0
HE1 B:HIS361 3.3 32.2 1.0
OE2 B:GLU389 3.3 25.5 1.0
HD2 B:HIS365 3.3 32.0 1.0
C12 B:FT8711 3.4 29.4 1.0
HE1 B:TYR501 3.6 30.5 1.0
HH B:TYR501 3.6 31.6 1.0
HA B:GLU389 3.8 29.8 1.0
N2 B:FT8711 4.0 26.0 1.0
C13 B:FT8711 4.2 36.2 1.0
ND1 B:HIS361 4.2 24.5 1.0
CG B:HIS361 4.2 22.1 1.0
ND1 B:HIS365 4.2 25.9 1.0
H11 B:BCN718 4.2 47.3 0.8
OE2 B:GLU362 4.2 27.0 1.0
CG B:HIS365 4.3 25.5 1.0
CG B:GLU389 4.3 23.3 1.0
OH B:TYR501 4.4 26.4 1.0
HB3 B:GLU389 4.4 29.8 1.0
C3 B:FT8711 4.4 26.7 1.0
CE1 B:TYR501 4.4 25.4 1.0
OE1 B:GLU362 4.6 27.7 1.0
O B:HOH914 4.6 28.4 1.0
CA B:GLU389 4.7 24.8 1.0
CB B:GLU389 4.7 24.8 1.0
CD B:GLU362 4.7 27.4 1.0
HG3 B:GLU389 4.8 28.0 1.0
CZ B:TYR501 4.9 26.4 1.0
HG2 B:GLU389 4.9 28.0 1.0
HD1 B:HIS361 4.9 29.4 1.0
H12 B:BCN718 5.0 47.3 0.8
HD1 B:HIS365 5.0 31.1 1.0
HA B:GLU362 5.0 27.8 1.0
C1 B:BCN718 5.0 39.4 0.8

Reference:

G.E.Cozier, L.Lubbe, E.D.Sturrock, K.R.Acharya. Ace-Domain Selectivity Extends Beyond Direct Interacting Residues at the Active Site. Biochem.J. 2020.
ISSN: ESSN 1470-8728
PubMed: 32195541
DOI: 10.1042/BCJ20200060
Page generated: Tue Oct 29 08:12:23 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy