Zinc in PDB 6zpq: Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain.

Enzymatic activity of Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain.

All present enzymatic activity of Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain.:
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain., PDB code: 6zpq 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) 80.50 / 1.85
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 74.683, 99.934, 128.701, 97.76, 90.21, 111.06
R / Rfree (%) 18.4 / 21.4

Other elements in 6zpq:

The structure of Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain. also contains other interesting chemical elements:

Magnesium (Mg) 3 atoms
Calcium (Ca) 4 atoms
Chlorine (Cl) 4 atoms
Sodium (Na) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain. (pdb code 6zpq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain., PDB code: 6zpq:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 6zpq

Go back to Zinc Binding Sites List in 6zpq
Zinc binding site 1 out of 4 in the Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain.


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 the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn719

b:28.7
occ:1.00
NE2 A:HIS361 2.0 24.5 1.0
OE1 A:GLU389 2.0 32.6 1.0
O A:HOH817 2.0 23.8 1.0
NE2 A:HIS365 2.1 24.9 1.0
CD A:GLU389 2.8 30.6 1.0
CD2 A:HIS361 2.9 27.3 1.0
CE1 A:HIS365 3.0 24.0 1.0
CE1 A:HIS361 3.0 29.5 1.0
OE2 A:GLU389 3.0 28.7 1.0
HD2 A:HIS361 3.1 32.8 1.0
CD2 A:HIS365 3.1 27.4 1.0
HE1 A:HIS365 3.1 28.7 1.0
HE1 A:HIS361 3.2 35.4 1.0
HD2 A:HIS365 3.3 32.9 1.0
O A:HOH1058 3.6 36.8 1.0
OE2 A:GLU362 3.7 30.0 1.0
HA A:GLU389 3.7 30.5 1.0
O A:HOH993 4.1 38.1 1.0
CG A:HIS361 4.1 26.4 1.0
ND1 A:HIS361 4.1 25.1 1.0
ND1 A:HIS365 4.1 24.2 1.0
CG A:HIS365 4.2 24.2 1.0
CG A:GLU389 4.2 29.8 1.0
O A:HOH910 4.3 39.1 1.0
CD A:GLU362 4.3 29.6 1.0
HG2 A:GLU389 4.3 35.7 1.0
O A:HOH1010 4.4 25.5 1.0
HA3 A:GLY392 4.5 31.6 1.0
OE1 A:GLU362 4.5 29.3 1.0
CA A:GLU389 4.6 25.4 1.0
HA A:GLU362 4.7 27.6 1.0
HG3 A:GLU389 4.8 35.7 1.0
HD1 A:HIS361 4.9 30.1 1.0
HD1 A:HIS365 4.9 29.0 1.0
CB A:GLU389 4.9 23.2 1.0
HO4 A:BCN707 5.0 51.6 1.0

Zinc binding site 2 out of 4 in 6zpq

Go back to Zinc Binding Sites List in 6zpq
Zinc binding site 2 out of 4 in the Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain.


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 the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn715

b:27.8
occ:1.00
O B:HOH860 1.9 25.0 1.0
NE2 B:HIS365 1.9 25.3 1.0
OE1 B:GLU389 2.1 23.7 1.0
NE2 B:HIS361 2.1 30.2 1.0
CE1 B:HIS365 2.9 31.3 1.0
CD B:GLU389 2.9 29.5 1.0
CD2 B:HIS361 2.9 28.3 1.0
HD2 B:HIS361 3.0 33.9 1.0
CD2 B:HIS365 3.0 30.2 1.0
HE1 B:HIS365 3.0 37.5 1.0
OE2 B:GLU389 3.1 23.6 1.0
CE1 B:HIS361 3.2 31.4 1.0
HD2 B:HIS365 3.3 36.2 1.0
HE1 B:HIS361 3.5 37.7 1.0
O B:HOH820 3.7 36.5 1.0
OE2 B:GLU362 3.7 29.6 1.0
O B:HOH1027 3.7 36.6 1.0
HA B:GLU389 3.8 29.6 1.0
ND1 B:HIS365 4.0 26.8 1.0
O B:HOH1123 4.0 51.8 1.0
CG B:HIS365 4.1 28.1 1.0
CG B:HIS361 4.2 25.4 1.0
ND1 B:HIS361 4.3 27.4 1.0
CG B:GLU389 4.3 25.0 1.0
CD B:GLU362 4.3 33.1 1.0
OE1 B:GLU362 4.3 31.0 1.0
O B:HOH910 4.4 26.1 1.0
O B:HOH834 4.4 34.4 1.0
HG2 B:GLU389 4.5 30.0 1.0
H42 B:BCN706 4.6 44.3 1.0
HA3 B:GLY392 4.6 24.8 1.0
CA B:GLU389 4.7 24.6 1.0
HA B:GLU362 4.7 29.6 1.0
HD1 B:HIS365 4.8 32.1 1.0
HG3 B:GLU389 4.9 30.0 1.0
CB B:GLU389 5.0 23.4 1.0

Zinc binding site 3 out of 4 in 6zpq

Go back to Zinc Binding Sites List in 6zpq
Zinc binding site 3 out of 4 in the Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn712

b:27.0
occ:1.00
O C:HOH815 2.0 24.0 1.0
NE2 C:HIS365 2.0 26.3 1.0
OE1 C:GLU389 2.0 24.8 1.0
NE2 C:HIS361 2.0 26.0 1.0
CD C:GLU389 2.9 28.4 1.0
CE1 C:HIS365 2.9 27.9 1.0
CD2 C:HIS361 2.9 23.8 1.0
HE1 C:HIS365 3.0 33.5 1.0
HD2 C:HIS361 3.1 28.6 1.0
CE1 C:HIS361 3.1 30.3 1.0
OE2 C:GLU389 3.1 25.3 1.0
CD2 C:HIS365 3.1 27.6 1.0
HE1 C:HIS361 3.3 36.3 1.0
HD2 C:HIS365 3.4 33.1 1.0
OE2 C:GLU362 3.6 28.0 1.0
HA C:GLU389 3.7 28.8 1.0
O C:HOH1056 3.8 34.8 1.0
O C:HOH888 3.8 41.4 1.0
O C:HOH1086 4.0 49.3 1.0
ND1 C:HIS365 4.1 24.4 1.0
CG C:HIS361 4.1 24.7 1.0
ND1 C:HIS361 4.2 25.7 1.0
CG C:HIS365 4.2 26.6 1.0
CD C:GLU362 4.3 29.4 1.0
CG C:GLU389 4.3 25.9 1.0
OE1 C:GLU362 4.4 25.9 1.0
O C:HOH836 4.4 34.2 1.0
HG2 C:GLU389 4.4 31.1 1.0
O C:HOH861 4.4 25.7 1.0
HA3 C:GLY392 4.6 29.7 1.0
CA C:GLU389 4.6 24.0 1.0
HA C:GLU362 4.7 28.5 1.0
HD1 C:HIS365 4.8 29.2 1.0
H42 C:BCN706 4.9 43.7 1.0
HG3 C:GLU389 4.9 31.1 1.0
HD1 C:HIS361 5.0 30.8 1.0

Zinc binding site 4 out of 4 in 6zpq

Go back to Zinc Binding Sites List in 6zpq
Zinc binding site 4 out of 4 in the Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of the Open Conformation of Angiotensin-1 Converting Enzyme N-Domain. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn715

b:28.0
occ:1.00
O D:HOH869 1.8 24.1 1.0
OE1 D:GLU389 2.0 27.5 1.0
NE2 D:HIS361 2.1 29.1 1.0
NE2 D:HIS365 2.1 26.6 1.0
CD D:GLU389 2.8 24.6 1.0
CD2 D:HIS361 2.9 27.8 1.0
HD2 D:HIS361 3.0 33.4 1.0
OE2 D:GLU389 3.0 26.3 1.0
CD2 D:HIS365 3.0 31.1 1.0
CE1 D:HIS365 3.1 26.9 1.0
HD2 D:HIS365 3.2 37.3 1.0
CE1 D:HIS361 3.2 28.9 1.0
HE1 D:HIS365 3.3 32.3 1.0
HE1 D:HIS361 3.5 34.7 1.0
O D:HOH1069 3.7 31.9 1.0
OE2 D:GLU362 3.7 30.9 1.0
O D:HOH815 3.7 39.2 1.0
HA D:GLU389 3.7 25.4 1.0
CG D:HIS361 4.1 26.1 1.0
O D:HOH990 4.1 53.1 1.0
ND1 D:HIS365 4.2 29.0 1.0
CG D:HIS365 4.2 30.4 1.0
HO1 D:EDO712 4.2 58.7 0.6
CG D:GLU389 4.2 28.2 1.0
ND1 D:HIS361 4.2 27.6 1.0
CD D:GLU362 4.3 40.8 1.0
HG2 D:GLU389 4.4 33.9 1.0
OE1 D:GLU362 4.4 31.6 1.0
O D:HOH964 4.4 31.5 1.0
O D:HOH825 4.4 38.5 1.0
HA3 D:GLY392 4.5 31.9 1.0
H11 D:EDO712 4.6 52.5 0.6
CA D:GLU389 4.6 21.2 1.0
HA D:GLU362 4.7 30.9 1.0
HG3 D:GLU389 4.8 33.9 1.0
HO4 D:BCN707 4.9 50.3 1.0
O1 D:EDO712 4.9 48.9 0.6
CB D:GLU389 5.0 23.6 1.0
HD1 D:HIS365 5.0 34.7 1.0

Reference:

G.E.Cozier, L.Lubbe, E.D.Sturrock, K.R.Acharya. Angiotensin-Converting Enzyme Open For Business: Structural Insights Into the Sub-Domain Dynamics. Febs J. 2020.
ISSN: ISSN 1742-464X
PubMed: 33067882
DOI: 10.1111/FEBS.15601
Page generated: Wed Dec 16 13:30:04 2020

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