Calcium in PDB 2blo: Elastase Before A High Dose X-Ray "Burn"

All present enzymatic activity of Elastase Before A High Dose X-Ray "Burn":
3.4.21.36;

The structure of Elastase Before A High Dose X-Ray "Burn", PDB code: 2blo was solved by M.H.Nanao, R.B.Ravelli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.00 / 1.33
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	49.767, 57.620, 74.075, 90.00, 90.00, 90.00
R / Rfree (%)	11.4 / 14

The binding sites of Calcium atom in the Elastase Before A High Dose X-Ray "Burn" (pdb code 2blo). 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 Elastase Before A High Dose X-Ray "Burn", PDB code: 2blo:

Calcium binding site 1 out of 1 in the Elastase Before A High Dose X-Ray "Burn"


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Elastase Before A High Dose X-Ray "Burn" within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1246 b:4.4 occ:0.49 OE2 A:GLU80 2.3 5.7 1.0 OE1 A:GLU70 2.3 8.0 1.0 O A:GLN75 2.3 10.4 1.0 O A:ASN72 2.4 6.2 1.0 OD1 A:ASP77 2.4 5.5 1.0 O A:HOH2071 2.6 19.1 1.0 CG A:ASP77 3.3 5.6 1.0 CD A:GLU70 3.4 5.9 1.0 CD A:GLU80 3.4 5.2 1.0 C A:ASN72 3.5 5.3 1.0 C A:GLN75 3.6 9.0 1.0 N A:ASP77 3.7 6.6 1.0 CG A:GLU80 3.8 5.3 1.0 OE2 A:GLU70 3.9 10.2 1.0 N A:ASN72 3.9 4.5 1.0 CB A:ASP77 4.0 5.8 1.0 CA A:ASN72 4.2 4.5 1.0 OD2 A:ASP77 4.2 7.0 1.0 CA A:ASN76 4.3 8.2 1.0 N A:ASN76 4.4 8.8 1.0 C A:ASN76 4.4 7.8 1.0 N A:GLN75 4.4 9.3 1.0 CB A:ASN72 4.4 5.9 1.0 CA A:ASP77 4.5 6.7 1.0 OE1 A:GLU80 4.5 6.1 1.0 N A:LEU73 4.5 5.7 1.0 N A:HIS71 4.6 3.7 1.0 CA A:GLN75 4.6 10.5 1.0 CG A:GLU70 4.6 4.9 1.0 CA A:LEU73 4.7 6.0 1.0 C A:LEU73 4.7 7.6 1.0 OH A:TYR82 4.7 12.3 1.0

M.H.Nanao, G.M.Sheldrick, R.B.Ravelli. Improving Radiation-Damage Substructures For Rip. Acta Crystallogr.,Sect.D V. 61 1227 2005.
ISSN: ISSN 0907-4449
PubMed: 16131756
DOI: 10.1107/S0907444905019360