Calcium in PDB 2g4v: Anomalous Substructure of Proteinase K

All present enzymatic activity of Anomalous Substructure of Proteinase K:
3.4.21.64;

The structure of Anomalous Substructure of Proteinase K, PDB code: 2g4v was solved by C.Mueller-Dieckmann, M.S.Weiss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.14
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	67.780, 67.780, 101.880, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / 20.3

The structure of Anomalous Substructure of Proteinase K also contains other interesting chemical elements:

Potassium	(K)	2 atoms
Chlorine	(Cl)	1 atom

The binding sites of Calcium atom in the Anomalous Substructure of Proteinase K (pdb code 2g4v). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Anomalous Substructure of Proteinase K, PDB code: 2g4v:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Anomalous Substructure of Proteinase K


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Anomalous Substructure of Proteinase K within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca280 b:17.8 occ:0.65 O A:VAL177 2.4 6.9 1.0 O A:PRO175 2.5 5.2 1.0 OD2 A:ASP200 2.5 8.0 1.0 O A:HOH383 2.5 9.5 1.0 OD1 A:ASP200 2.7 7.9 1.0 CA A:CA281 2.7 2.0 0.3 CG A:ASP200 2.9 7.0 1.0 C A:PRO175 3.5 6.1 1.0 C A:VAL177 3.6 6.2 1.0 N A:VAL177 4.0 5.0 1.0 CA A:PRO175 4.3 5.7 1.0 CB A:ASP200 4.3 5.9 1.0 N A:SER176 4.4 4.5 1.0 C A:SER176 4.4 5.9 1.0 CA A:CYS178 4.4 6.9 1.0 O A:GLU174 4.5 3.5 1.0 O A:VAL198 4.5 9.6 1.0 N A:CYS178 4.5 6.5 1.0 CA A:VAL177 4.5 4.9 1.0 CA A:SER176 4.6 5.2 1.0 N A:THR179 4.7 5.5 1.0 SG A:CYS249 4.7 5.5 1.0 O A:SER176 5.0 6.2 1.0

Calcium binding site 2 out of 2 in the Anomalous Substructure of Proteinase K


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Anomalous Substructure of Proteinase K within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca281 b:2.0 occ:0.35 OG1 A:THR179 2.7 7.9 1.0 CA A:CA280 2.7 17.8 0.7 O A:GLU174 2.8 3.5 1.0 OD2 A:ASP200 2.9 8.0 1.0 O A:VAL177 3.0 6.9 1.0 O A:VAL198 3.2 9.6 1.0 CB A:THR179 3.4 6.5 1.0 O A:PRO175 3.6 5.2 1.0 CG2 A:VAL198 3.7 12.9 1.0 N A:THR179 3.8 5.5 1.0 C A:GLU174 3.8 3.6 1.0 C A:VAL177 3.8 6.2 1.0 C A:PRO175 3.9 6.1 1.0 CA A:PRO175 3.9 5.7 1.0 O A:ALA172 4.0 5.9 1.0 CG A:ASP200 4.0 7.0 1.0 CG2 A:VAL177 4.2 4.0 1.0 CA A:THR179 4.3 6.1 1.0 N A:VAL177 4.3 5.0 1.0 N A:PRO175 4.3 4.9 1.0 C A:VAL198 4.3 8.5 1.0 OD1 A:ASP200 4.4 7.9 1.0 C A:CYS178 4.5 6.4 1.0 N A:CYS178 4.6 6.5 1.0 CG2 A:THR179 4.6 2.0 1.0 CA A:VAL177 4.6 4.9 1.0 CA A:CYS178 4.7 6.9 1.0 N A:SER176 4.7 4.5 1.0 CB A:VAL198 4.8 6.6 1.0 N A:GLU174 5.0 3.9 1.0 CA A:VAL198 5.0 8.2 1.0

C.Mueller-Dieckmann, S.Panjikar, A.Schmidt, S.Mueller, J.Kuper, A.Geerlof, M.Wilmanns, R.K.Singh, P.A.Tucker, M.S.Weiss. On the Routine Use of Soft X-Rays in Macromolecular Crystallography. Part IV. Efficient Determination of Anomalous Substructures in Biomacromolecules Using Longer X-Ray Wavelengths. Acta Crystallogr.,Sect.D V. 63 366 2007.
ISSN: ISSN 0907-4449
PubMed: 17327674
DOI: 10.1107/S0907444906055624