Calcium in PDB 3n0a: Crystal Structure of Auxilin (40-400)

All present enzymatic activity of Crystal Structure of Auxilin (40-400):
3.1.3.48;

The structure of Crystal Structure of Auxilin (40-400), PDB code: 3n0a was solved by S.C.Harrison, R.Guan, H.Dai, T.Kirchhausen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.90 / 2.20
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	137.925, 137.925, 51.327, 90.00, 90.00, 120.00
R / Rfree (%)	17.2 / 20

The structure of Crystal Structure of Auxilin (40-400) also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Calcium atom in the Crystal Structure of Auxilin (40-400) (pdb code 3n0a). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Auxilin (40-400), PDB code: 3n0a:

Calcium binding site 1 out of 1 in the Crystal Structure of Auxilin (40-400)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Auxilin (40-400) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:66.9 occ:1.00 OD1 A:ASN180 2.5 52.3 1.0 O A:LEU216 2.5 46.8 1.0 O A:HOH654 2.7 43.0 1.0 O A:HOH580 2.8 59.1 1.0 O A:HOH653 2.9 50.6 1.0 O A:HOH669 2.9 68.2 1.0 O A:HOH557 3.0 53.6 1.0 CG A:ASN180 3.5 50.5 1.0 C A:LEU216 3.6 42.9 1.0 ND2 A:ASN180 4.0 52.1 1.0 OG1 A:THR380 4.1 78.2 1.0 CB A:LEU216 4.1 36.3 1.0 O A:HOH562 4.3 47.1 1.0 CA A:LEU216 4.4 40.5 1.0 O A:ILE177 4.5 33.2 1.0 N A:ALA217 4.6 44.0 1.0 O A:HOH700 4.6 66.7 1.0 CA A:ALA217 4.6 47.5 1.0 CB A:ASN180 4.7 41.6 1.0 OG A:SER183 4.7 65.4 1.0 C A:ALA217 4.7 50.1 1.0 CA A:ASN180 4.8 36.5 1.0 CB A:THR380 4.8 75.1 1.0 OD1 A:ASP218 4.9 74.3 1.0 N A:ASP218 5.0 59.0 1.0

R.Guan, D.Han, S.C.Harrison, T.Kirchhausen. Structure of the Pten-Like Region of Auxilin, A Detector of Clathrin-Coated Vesicle Budding. Structure V. 18 1191 2010.
ISSN: ISSN 0969-2126
PubMed: 20826345
DOI: 10.1016/J.STR.2010.06.016