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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

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