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Zinc in PDB 4h2f: Human Ecto-5'-Nucleotidase (CD73): Crystal Form I (Open) in Complex with Adenosine

Enzymatic activity of Human Ecto-5'-Nucleotidase (CD73): Crystal Form I (Open) in Complex with Adenosine

All present enzymatic activity of Human Ecto-5'-Nucleotidase (CD73): Crystal Form I (Open) in Complex with Adenosine:
3.1.3.5;

Protein crystallography data

The structure of Human Ecto-5'-Nucleotidase (CD73): Crystal Form I (Open) in Complex with Adenosine, PDB code: 4h2f was solved by N.Straeter, K.M.Knapp, M.Zebisch, J.Pippel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.89 / 1.85
Space group P 43 3 2
Cell size a, b, c (Å), α, β, γ (°) 167.548, 167.548, 167.548, 90.00, 90.00, 90.00
R / Rfree (%) 15.7 / 17.9

Other elements in 4h2f:

The structure of Human Ecto-5'-Nucleotidase (CD73): Crystal Form I (Open) in Complex with Adenosine also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Calcium (Ca) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Ecto-5'-Nucleotidase (CD73): Crystal Form I (Open) in Complex with Adenosine (pdb code 4h2f). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Human Ecto-5'-Nucleotidase (CD73): Crystal Form I (Open) in Complex with Adenosine, PDB code: 4h2f:

Zinc binding site 1 out of 1 in 4h2f

Go back to Zinc Binding Sites List in 4h2f
Zinc binding site 1 out of 1 in the Human Ecto-5'-Nucleotidase (CD73): Crystal Form I (Open) in Complex with Adenosine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Ecto-5'-Nucleotidase (CD73): Crystal Form I (Open) in Complex with Adenosine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn602

b:18.9
occ:1.00
 NE2 A:HIS220 2.0 14.6 1.0
OD1 A:ASN117 2.0 17.5 1.0
O A:HOH703 2.1 38.5 1.0
OD2 A:ASP85 2.1 16.9 1.0
ND1 A:HIS243 2.1 18.6 1.0
CE1 A:HIS243 2.9 21.3 1.0
CD2 A:HIS220 3.0 15.3 1.0
CG A:ASP85 3.0 17.5 1.0
CE1 A:HIS220 3.0 13.9 1.0
CG A:ASN117 3.1 18.7 1.0
CG A:HIS243 3.3 18.4 1.0
OD1 A:ASP85 3.3 17.9 1.0
O A:HOH769 3.4 22.3 1.0
ND2 A:ASN117 3.5 18.8 1.0
CA A:HIS243 3.6 16.6 1.0
O A:ASP377 3.7 29.8 1.0
CB A:HIS243 3.8 17.3 1.0
OD1 A:ASP36 3.9 18.4 1.0
NE2 A:HIS243 4.1 20.4 1.0
CG A:HIS220 4.1 15.0 1.0
ND1 A:HIS220 4.1 14.4 1.0
N A:ASN117 4.2 18.9 1.0
O A:HIS243 4.3 20.0 1.0
CD2 A:HIS243 4.3 19.4 1.0
CB A:ASP85 4.3 16.0 1.0
CB A:ASN117 4.4 19.7 1.0
C A:HIS243 4.5 17.6 1.0
N A:HIS243 4.7 15.2 1.0
CD2 A:HIS118 4.7 24.7 1.0
O A:HOH874 4.8 31.1 1.0
C A:ASP377 4.8 27.8 1.0
CA A:ASN117 4.9 20.3 1.0

Reference:

K.Knapp, M.Zebisch, J.Pippel, A.El-Tayeb, C.E.Muller, N.Strater. Crystal Structure of the Human Ecto-5'-Nucleotidase (CD73): Insights Into the Regulation of Purinergic Signaling. Structure V. 20 2161 2012.
ISSN: ISSN 0969-2126
PubMed: 23142347
DOI: 10.1016/J.STR.2012.10.001
Page generated: Wed Dec 16 05:21:29 2020

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