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Zinc in PDB 5luz: Structure of Human Neurolysin (E475Q) in Complex with Neurotensin Peptide Products

Enzymatic activity of Structure of Human Neurolysin (E475Q) in Complex with Neurotensin Peptide Products

All present enzymatic activity of Structure of Human Neurolysin (E475Q) in Complex with Neurotensin Peptide Products:
3.4.24.16;

Protein crystallography data

The structure of Structure of Human Neurolysin (E475Q) in Complex with Neurotensin Peptide Products, PDB code: 5luz 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) 50.00 / 2.70
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 131.329, 131.329, 195.229, 90.00, 90.00, 90.00
R / Rfree (%) 21.6 / 26.8

Other elements in 5luz:

The structure of Structure of Human Neurolysin (E475Q) in Complex with Neurotensin Peptide Products 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 Neurotensin Peptide Products (pdb code 5luz). 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 Neurotensin Peptide Products, PDB code: 5luz:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5luz

Go back to Zinc Binding Sites List in 5luz
Zinc binding site 1 out of 2 in the Structure of Human Neurolysin (E475Q) in Complex with Neurotensin Peptide Products


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 Neurotensin Peptide Products within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:50.7
occ:1.00
OE1 A:GLU503 2.2 34.8 1.0
NE2 A:HIS478 2.6 37.7 1.0
NE2 A:HIS474 2.6 40.7 1.0
CD A:GLU503 2.9 35.1 1.0
OE2 A:GLU503 2.9 34.4 1.0
C C:PRO10 3.2 77.2 1.0
CD2 A:HIS474 3.3 40.5 1.0
CD2 A:HIS478 3.4 37.8 1.0
CE1 A:HIS474 3.5 40.9 1.0
CE1 A:HIS478 3.6 38.0 1.0
O C:PRO10 3.6 75.5 1.0
NE2 A:GLN475 3.9 39.2 1.0
OG A:SER506 3.9 39.4 1.0
CB A:SER506 4.3 39.4 1.0
CA C:PRO10 4.4 78.5 1.0
CG A:GLU503 4.4 35.6 1.0
CG A:HIS474 4.4 40.4 1.0
ND1 A:HIS474 4.5 40.9 1.0
CG A:HIS478 4.6 38.1 1.0
ND1 A:HIS478 4.6 38.4 1.0
CD A:GLN475 4.7 38.8 1.0
CE1 A:TYR613 4.7 33.8 1.0
N C:PRO10 4.8 78.6 1.0
OE1 A:GLN475 4.8 39.1 1.0
O C:ARG9 4.8 78.8 1.0
C C:ARG9 4.9 79.7 1.0

Zinc binding site 2 out of 2 in 5luz

Go back to Zinc Binding Sites List in 5luz
Zinc binding site 2 out of 2 in the Structure of Human Neurolysin (E475Q) in Complex with Neurotensin Peptide Products


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 Neurotensin Peptide Products within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1001

b:54.6
occ:1.00
O D:PRO9 2.1 69.1 1.0
OE1 B:GLU503 2.3 41.7 1.0
NE2 B:HIS478 2.4 43.9 1.0
NE2 B:HIS474 2.6 47.3 1.0
OE2 B:GLU503 2.8 42.7 1.0
CD B:GLU503 2.9 42.8 1.0
C D:PRO9 3.3 69.0 1.0
CE1 B:HIS478 3.4 43.8 1.0
CD2 B:HIS474 3.4 47.3 1.0
CD2 B:HIS478 3.4 44.1 1.0
CE1 B:HIS474 3.6 47.9 1.0
OG B:SER506 3.9 47.1 1.0
OE1 B:GLN475 4.1 49.6 1.0
O D:ARG8 4.2 71.0 1.0
CB B:SER506 4.2 47.3 1.0
CA D:PRO9 4.3 69.5 1.0
CE1 B:TYR613 4.3 36.6 1.0
CG B:GLU503 4.4 42.9 1.0
ND1 B:HIS478 4.5 44.5 1.0
CG B:HIS478 4.5 44.5 1.0
C D:ARG8 4.5 70.4 1.0
CG B:HIS474 4.6 47.9 1.0
N D:PRO9 4.6 69.9 1.0
ND1 B:HIS474 4.7 48.1 1.0
NE2 B:GLN475 4.7 49.5 1.0
CD B:GLN475 4.8 49.1 1.0
OH B:TYR613 4.9 36.5 1.0
OH B:TYR606 4.9 39.8 1.0

Reference:

P.F.Teixeira, G.Masuyer, C.M.Pinho, R.M.M.Branca, B.Kmiec, C.Wallin, S.K.T.S.Warmlander, R.P.Berntsson, M.Ankarcrona, A.Graslund, J.Lehtio, P.Stenmark, E.Glaser. Mechanism of Peptide Binding and Cleavage By the Human Mitochondrial Peptidase Neurolysin. J. Mol. Biol. V. 430 348 2018.
ISSN: ESSN 1089-8638
PubMed: 29183787
DOI: 10.1016/J.JMB.2017.11.011
Page generated: Wed Dec 16 06:30:52 2020

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