Calcium in PDB 8f07: Proteinase K Anomalous Dataset at 273 K and 12 Kev

All present enzymatic activity of Proteinase K Anomalous Dataset at 273 K and 12 Kev:
3.4.21.64;

The structure of Proteinase K Anomalous Dataset at 273 K and 12 Kev, PDB code: 8f07 was solved by T.Doukov, F.Yabukarski, D.Herschlag, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.37 / 1.05
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	68.382, 68.382, 103.558, 90, 90, 90
R / Rfree (%)	9.6 / 10.5

The binding sites of Calcium atom in the Proteinase K Anomalous Dataset at 273 K and 12 Kev (pdb code 8f07). 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 Proteinase K Anomalous Dataset at 273 K and 12 Kev, PDB code: 8f07:

Calcium binding site 1 out of 1 in the Proteinase K Anomalous Dataset at 273 K and 12 Kev


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Proteinase K Anomalous Dataset at 273 K and 12 Kev within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca301 b:9.8 occ:0.25 O A:HOH559 1.8 14.6 0.8 OD2 A:ASP200 2.4 7.4 1.0 O A:HOH562 2.4 11.4 1.0 O A:VAL177 2.5 7.9 1.0 O A:HOH641 2.5 26.8 1.0 O A:PRO175 2.5 10.1 1.0 O A:HOH588 2.5 41.9 1.0 OD1 A:ASP200 2.7 13.3 1.0 CG A:ASP200 2.9 7.2 1.0 C A:PRO175 3.6 8.1 1.0 C A:VAL177 3.7 5.8 1.0 CA A:PRO175 4.2 9.0 1.0 N A:VAL177 4.3 6.7 1.0 CB A:ASP200 4.4 6.7 1.0 O A:VAL198 4.4 10.3 1.0 O A:GLU174 4.4 7.6 1.0 O A:HOH579 4.4 28.5 1.0 O A:HOH664 4.4 36.1 1.0 CA A:CYS178 4.5 5.3 1.0 O A:HOH572 4.5 18.9 1.0 N A:CYS178 4.5 5.6 1.0 N A:SER176 4.5 7.7 1.0 C A:SER176 4.5 7.5 1.0 CA A:VAL177 4.6 6.6 1.0 N A:THR179 4.7 5.0 1.0 CA A:SER176 4.8 8.1 1.0 SG A:CYS249 4.9 8.0 1.0 OG1 A:THR179 4.9 7.2 1.0

T.Doukov, D.Herschlag, F.Yabukarski. Obtaining Anomalous and Ensemble Information From Protein Crystals From 220 K Up to Physiological Temperatures. Acta Crystallogr D Struct V. 79 212 2023BIOL.
ISSN: ISSN 2059-7983
PubMed: 36876431
DOI: 10.1107/S205979832300089X