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Zinc in PDB 5lv0: Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product

Enzymatic activity of Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product

All present enzymatic activity of Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product:
3.4.24.16;

Protein crystallography data

The structure of Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product, PDB code: 5lv0 was solved by G.Masuyer, R.P.-A.Berntsson, P.F.Teixeira, B.Kmiec, E.Glaser, P.Stenmark, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 109.11 / 2.70
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 131.341, 131.341, 195.979, 90.00, 90.00, 90.00
R / Rfree (%) 21 / 26

Other elements in 5lv0:

The structure of Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product (pdb code 5lv0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product, PDB code: 5lv0:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5lv0

Go back to Zinc Binding Sites List in 5lv0
Zinc binding site 1 out of 2 in the Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn701

b:46.4
occ:1.00
OE1 A:GLU503 2.1 43.8 1.0
NE2 A:HIS478 2.3 45.4 1.0
NE2 A:HIS474 2.4 48.3 1.0
OXT C:VAL6 2.7 72.7 1.0
O C:VAL6 2.7 73.7 1.0
CD A:GLU503 2.9 44.0 1.0
OE2 A:GLU503 2.9 43.2 1.0
CD2 A:HIS474 3.0 48.4 1.0
C C:VAL6 3.0 71.8 1.0
CD2 A:HIS478 3.1 45.8 1.0
CE1 A:HIS478 3.4 46.0 1.0
CE1 A:HIS474 3.6 48.7 1.0
OG A:SER506 3.7 48.0 1.0
O C:VAL5 3.9 66.9 1.0
CB A:SER506 4.0 48.2 1.0
CG A:HIS474 4.2 49.0 1.0
NE2 A:GLN475 4.3 48.9 1.0
CA C:VAL6 4.3 70.5 1.0
CG A:GLU503 4.3 44.4 1.0
CE1 A:TYR613 4.3 47.0 1.0
CG A:HIS478 4.4 46.5 1.0
C C:VAL5 4.4 68.1 1.0
N C:VAL6 4.4 70.0 1.0
ND1 A:HIS478 4.5 46.5 1.0
ND1 A:HIS474 4.5 49.1 1.0
OE1 A:GLN475 4.6 47.6 1.0
OH A:TYR613 4.6 47.4 1.0
CD A:GLN475 4.8 48.2 1.0
CZ A:TYR613 4.9 47.1 1.0
OH A:TYR606 5.0 45.0 1.0
CB A:GLU503 5.0 44.6 1.0
CG1 C:VAL5 5.0 68.3 1.0

Zinc binding site 2 out of 2 in 5lv0

Go back to Zinc Binding Sites List in 5lv0
Zinc binding site 2 out of 2 in the Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Human Neurolysin (E475Q) in Complex with Amyloid-Beta 35- 40 Peptide Product within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn701

b:46.7
occ:1.00
OE1 B:GLU503 2.2 45.8 1.0
NE2 B:HIS474 2.3 50.7 1.0
NE2 B:HIS478 2.4 47.0 1.0
O D:VAL6 2.5 74.9 1.0
OE2 B:GLU503 2.7 46.4 1.0
CD B:GLU503 2.8 46.3 1.0
OXT D:VAL6 2.8 73.4 1.0
C D:VAL6 3.0 72.7 1.0
CD2 B:HIS474 3.1 50.7 1.0
CE1 B:HIS478 3.3 47.3 1.0
CD2 B:HIS478 3.4 47.5 1.0
CE1 B:HIS474 3.4 51.0 1.0
OG B:SER506 3.7 51.3 1.0
CB B:SER506 4.1 51.8 1.0
CE2 B:TYR613 4.2 44.6 1.0
CG B:GLU503 4.3 46.6 1.0
NE2 B:GLN475 4.3 55.3 1.0
CG B:HIS474 4.3 51.5 1.0
CA D:VAL6 4.4 71.7 1.0
OH B:TYR613 4.4 44.4 1.0
ND1 B:HIS478 4.4 48.0 1.0
O D:VAL5 4.4 68.8 1.0
ND1 B:HIS474 4.5 51.4 1.0
CG B:HIS478 4.5 48.2 1.0
N D:VAL6 4.6 71.4 1.0
CZ B:TYR613 4.7 44.7 1.0
C D:VAL5 4.7 69.3 1.0
OH B:TYR606 4.8 42.9 1.0
CB B:GLU503 5.0 47.3 1.0
CG1 D:VAL5 5.0 69.2 1.0
OE1 B:GLN475 5.0 55.3 1.0

Reference:

P.F.Teixeira, G.Masuyer, C.Pinho, R.M.M.Branca, B.Kmiec, C.Wallin, S.Warmlander, R.P.-A.Berntsson, M.Ankarcrona, A.Graslund, J.Lehtio, P.Stenmark, E.Glaser. Structural and Functional Analysis of Neurolysin, A New Component of the Mitochondrial Peptidolytic Network To Be Published.
Page generated: Wed Dec 16 06:30:54 2020

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