Atomistry » Zinc » PDB 6zpf-6zxd » 6zpq
Atomistry »
  Zinc »
    PDB 6zpf-6zxd »
      6zpq »

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: Tue Oct 29 15:52:51 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy