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Zinc in PDB 4ufb: Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro

Enzymatic activity of Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro

All present enzymatic activity of Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro:
3.4.15.1;

Protein crystallography data

The structure of Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro, PDB code: 4ufb was solved by G.Masuyer, R.G.Douglas, E.D.Sturrock, K.R.Acharya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 113.94 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 73.480, 101.590, 114.510, 85.46, 85.90, 81.62
R / Rfree (%) 20.7 / 23.5

Other elements in 4ufb:

The structure of Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro (pdb code 4ufb). 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 Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro, PDB code: 4ufb:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 4ufb

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Zinc binding site 1 out of 4 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro


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 Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:21.2
occ:1.00
 O A:HOH2270 2.0 17.6 1.0
OE1 A:GLU389 2.0 21.2 1.0
NE2 A:HIS361 2.0 19.6 1.0
NE2 A:HIS365 2.0 20.6 1.0
CD A:GLU389 3.0 21.2 1.0
CD2 A:HIS361 3.0 19.5 1.0
CE1 A:HIS365 3.0 20.7 1.0
CE1 A:HIS361 3.0 19.8 1.0
CD2 A:HIS365 3.0 20.8 1.0
OE2 A:GLU389 3.2 21.2 1.0
N A:LYS1303 3.9 24.1 1.0
O A:HOH2252 3.9 33.5 1.0
CE1 A:TYR501 4.1 20.7 1.0
ND1 A:HIS361 4.1 19.6 1.0
CG A:HIS361 4.1 19.7 1.0
ND1 A:HIS365 4.1 20.7 1.0
CG A:HIS365 4.2 21.0 1.0
OH A:TYR501 4.2 22.0 1.0
CA A:LYS1303 4.2 24.4 1.0
CG A:GLU389 4.3 21.3 1.0
O A:HOH2279 4.4 20.4 1.0
OE1 A:GLU362 4.6 20.6 1.0
OE2 A:GLU362 4.6 21.0 1.0
CA A:GLU389 4.6 21.3 1.0
CZ A:TYR501 4.6 21.2 1.0
C A:LYS1303 4.7 23.9 1.0
CB A:GLU389 4.7 20.9 1.0
CD A:GLU362 4.9 20.6 1.0
O A:HOH2251 4.9 33.9 1.0

Zinc binding site 2 out of 4 in 4ufb

Go back to Zinc Binding Sites List in 4ufb
Zinc binding site 2 out of 4 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro


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 Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:21.7
occ:1.00
 OE1 B:GLU389 2.0 19.2 1.0
NE2 B:HIS365 2.0 20.0 1.0
O B:HOH2260 2.1 18.5 1.0
NE2 B:HIS361 2.1 18.9 1.0
CD B:GLU389 2.9 19.5 1.0
CE1 B:HIS365 2.9 20.2 1.0
CE1 B:HIS361 3.1 18.5 1.0
CD2 B:HIS361 3.1 18.9 1.0
CD2 B:HIS365 3.1 19.8 1.0
OE2 B:GLU389 3.2 19.1 1.0
N B:LYS1303 3.9 24.9 1.0
O B:HOH2241 4.0 31.3 1.0
CE1 B:TYR501 4.1 19.7 1.0
ND1 B:HIS365 4.1 19.9 1.0
CA B:LYS1303 4.1 24.4 1.0
ND1 B:HIS361 4.1 18.6 1.0
CG B:HIS365 4.2 19.6 1.0
CG B:HIS361 4.2 18.8 1.0
OH B:TYR501 4.3 19.6 1.0
CG B:GLU389 4.3 19.7 1.0
O B:HOH2270 4.4 17.4 1.0
C4 B:PEG1205 4.4 63.0 1.0
CA B:GLU389 4.6 20.6 1.0
OE1 B:GLU362 4.6 21.3 1.0
O B:HOH2240 4.6 47.0 1.0
OE2 B:GLU362 4.6 22.1 1.0
CZ B:TYR501 4.7 19.6 1.0
C B:LYS1303 4.7 24.1 1.0
CB B:GLU389 4.7 20.3 1.0
CD B:GLU362 4.9 21.2 1.0
CD B:PRO1304 5.0 24.0 1.0

Zinc binding site 3 out of 4 in 4ufb

Go back to Zinc Binding Sites List in 4ufb
Zinc binding site 3 out of 4 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro


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 Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn1001

b:19.8
occ:1.00
 OE1 C:GLU389 1.9 17.9 1.0
NE2 C:HIS365 2.0 17.6 1.0
NE2 C:HIS361 2.1 17.6 1.0
O C:HOH2299 2.1 16.9 1.0
CE1 C:HIS365 2.9 17.4 1.0
CD C:GLU389 2.9 17.9 1.0
CE1 C:HIS361 3.0 17.8 1.0
CD2 C:HIS361 3.1 17.1 1.0
CD2 C:HIS365 3.1 17.7 1.0
OE2 C:GLU389 3.2 18.1 1.0
O C:HOH2279 3.8 35.4 1.0
N C:LYS1303 4.0 24.8 1.0
CE1 C:TYR501 4.0 16.9 1.0
ND1 C:HIS365 4.0 17.6 1.0
ND1 C:HIS361 4.1 17.0 1.0
CG C:HIS365 4.2 17.7 1.0
CA C:LYS1303 4.2 24.4 1.0
CG C:HIS361 4.2 17.2 1.0
OH C:TYR501 4.2 17.3 1.0
CG C:GLU389 4.3 17.6 1.0
O C:HOH2310 4.4 18.5 1.0
CA C:GLU389 4.6 17.4 1.0
OE2 C:GLU362 4.6 20.0 1.0
CZ C:TYR501 4.6 17.1 1.0
OE1 C:GLU362 4.7 20.5 1.0
CB C:GLU389 4.7 17.4 1.0
C C:LYS1303 4.7 24.0 1.0
C12 C:P6G1202 4.9 47.9 1.0
O C:HOH2278 4.9 33.5 1.0
CD C:GLU362 4.9 19.7 1.0

Zinc binding site 4 out of 4 in 4ufb

Go back to Zinc Binding Sites List in 4ufb
Zinc binding site 4 out of 4 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro


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 Angiotensin-1 Converting Enzyme N-Domain in Complex with Lys-Pro within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn1001

b:20.0
occ:1.00
 OE1 D:GLU389 2.0 18.2 1.0
NE2 D:HIS365 2.0 17.6 1.0
NE2 D:HIS361 2.1 18.1 1.0
O D:HOH2304 2.1 13.4 1.0
CE1 D:HIS361 3.0 17.9 1.0
CE1 D:HIS365 3.0 17.4 1.0
CD D:GLU389 3.0 17.9 1.0
CD2 D:HIS365 3.1 17.5 1.0
CD2 D:HIS361 3.1 17.6 1.0
OE2 D:GLU389 3.3 18.1 1.0
O D:HOH2284 3.8 27.6 1.0
N D:LYS1303 3.9 22.3 1.0
CE1 D:TYR501 4.0 17.3 1.0
ND1 D:HIS361 4.1 17.4 1.0
ND1 D:HIS365 4.1 17.7 1.0
CG D:HIS361 4.2 17.4 1.0
OH D:TYR501 4.2 18.4 1.0
CG D:HIS365 4.2 17.7 1.0
CG D:GLU389 4.4 17.8 1.0
O D:HOH2314 4.4 18.3 1.0
CA D:LYS1303 4.4 22.6 1.0
OE1 D:GLU362 4.5 19.3 1.0
CA D:GLU389 4.6 17.6 1.0
CZ D:TYR501 4.6 17.7 1.0
O D:HOH2283 4.7 38.0 1.0
OE2 D:GLU362 4.7 19.6 1.0
CB D:GLU389 4.7 17.9 1.0
C D:LYS1303 4.8 21.8 1.0
C12 D:P6G1202 4.9 54.7 1.0
CD D:GLU362 4.9 18.7 1.0

Reference:

G.Masuyer, R.G.Douglas, E.D.Sturrock, K.R.Acharya. Structural Basis of Ac-Sdkp Hydrolysis By Angiotensin-I Converting Enzyme Sci.Rep. V. 5 13742 2015.
ISSN: ESSN 2045-2322
PubMed: 26403559
DOI: 10.1038/SREP13742
Page generated: Sun Oct 27 09:04:47 2024

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