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Calcium in PDB 2prk: Synchrotron X-Ray Data Collection and Restrained Least-Squares Refinement of the Crystal Structure of Proteinase K at 1.5 Angstroms Resolution

Enzymatic activity of Synchrotron X-Ray Data Collection and Restrained Least-Squares Refinement of the Crystal Structure of Proteinase K at 1.5 Angstroms Resolution

All present enzymatic activity of Synchrotron X-Ray Data Collection and Restrained Least-Squares Refinement of the Crystal Structure of Proteinase K at 1.5 Angstroms Resolution:
3.4.21.14;

Protein crystallography data

The structure of Synchrotron X-Ray Data Collection and Restrained Least-Squares Refinement of the Crystal Structure of Proteinase K at 1.5 Angstroms Resolution, PDB code: 2prk was solved by C.Betzel, G.P.Pal, W.Saenger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.50
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 68.170, 68.170, 108.260, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Synchrotron X-Ray Data Collection and Restrained Least-Squares Refinement of the Crystal Structure of Proteinase K at 1.5 Angstroms Resolution (pdb code 2prk). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Synchrotron X-Ray Data Collection and Restrained Least-Squares Refinement of the Crystal Structure of Proteinase K at 1.5 Angstroms Resolution, PDB code: 2prk:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 2prk

Go back to Calcium Binding Sites List in 2prk
Calcium binding site 1 out of 2 in the Synchrotron X-Ray Data Collection and Restrained Least-Squares Refinement of the Crystal Structure of Proteinase K at 1.5 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Synchrotron X-Ray Data Collection and Restrained Least-Squares Refinement of the Crystal Structure of Proteinase K at 1.5 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca280

b:6.7
occ:1.00
 O A:PRO175 2.4 5.2 1.0
O A:HOH283 2.4 12.6 1.0
O A:HOH285 2.4 7.8 1.0
O A:VAL177 2.5 5.5 1.0
O A:HOH284 2.5 7.7 1.0
OD1 A:ASP200 2.5 6.7 1.0
O A:HOH282 2.5 9.4 1.0
OD2 A:ASP200 2.7 8.3 1.0
CG A:ASP200 2.9 7.5 1.0
C A:PRO175 3.5 6.2 1.0
C A:VAL177 3.7 5.2 1.0
CA A:PRO175 4.2 7.3 1.0
O A:HOH396 4.2 31.2 1.0
N A:VAL177 4.2 5.6 1.0
O A:VAL198 4.3 9.3 1.0
O A:HOH446 4.4 27.9 1.0
CB A:ASP200 4.4 6.2 1.0
C A:SER176 4.5 5.4 1.0
N A:SER176 4.5 4.9 1.0
CA A:CYS178 4.5 5.1 1.0
O A:GLU174 4.6 6.2 1.0
N A:CYS178 4.6 4.6 1.0
N A:THR179 4.6 4.5 1.0
CA A:VAL177 4.7 4.5 1.0
CA A:SER176 4.8 6.0 1.0
O A:HOH296 4.8 13.3 1.0
OG1 A:THR179 4.8 4.8 1.0
SG A:CYS249 5.0 8.2 1.0

Calcium binding site 2 out of 2 in 2prk

Go back to Calcium Binding Sites List in 2prk
Calcium binding site 2 out of 2 in the Synchrotron X-Ray Data Collection and Restrained Least-Squares Refinement of the Crystal Structure of Proteinase K at 1.5 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Synchrotron X-Ray Data Collection and Restrained Least-Squares Refinement of the Crystal Structure of Proteinase K at 1.5 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca281

b:10.9
occ:1.00
 O A:THR16 2.4 16.1 1.0
O A:HOH287 2.5 26.0 1.0
O A:HOH286 2.5 22.4 1.0
OD1 A:ASP260 2.5 18.1 1.0
OD2 A:ASP260 2.5 17.3 1.0
CG A:ASP260 2.9 16.7 1.0
C A:THR16 3.6 15.9 1.0
CB A:ASP260 4.3 14.2 1.0
CA A:THR16 4.5 14.9 1.0
ND2 A:ASN257 4.5 8.9 1.0
N A:SER17 4.6 15.9 1.0
NH2 A:ARG12 4.7 7.9 1.0
CG2 A:THR16 4.7 16.7 1.0
CA A:SER17 4.8 15.7 1.0
CG A:ASN257 4.8 8.9 1.0
CB A:THR16 5.0 16.6 1.0
CB A:ASN257 5.0 8.0 1.0

Reference:

C.Betzel, G.P.Pal, W.Saenger. Synchrotron X-Ray Data Collection and Restrained Least-Squares Refinement of the Crystal Structure of Proteinase K at 1.5 A Resolution. Acta Crystallogr.,Sect.B V. 44 163 1988.
ISSN: ISSN 0108-7681
PubMed: 3271105
DOI: 10.1107/S010876818700939X
Page generated: Tue Jul 8 07:46:27 2025

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