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Calcium in PDB 2pq2: Structure of Serine Proteinase K Complex with A Highly Flexible Hydrophobic Peptide at 1.8A Resolution

Enzymatic activity of Structure of Serine Proteinase K Complex with A Highly Flexible Hydrophobic Peptide at 1.8A Resolution

All present enzymatic activity of Structure of Serine Proteinase K Complex with A Highly Flexible Hydrophobic Peptide at 1.8A Resolution:
3.4.21.64;

Protein crystallography data

The structure of Structure of Serine Proteinase K Complex with A Highly Flexible Hydrophobic Peptide at 1.8A Resolution, PDB code: 2pq2 was solved by A.S.Ethayathulla, A.K.Singh, N.Singh, S.Sharma, M.Sinha, R.K.Somvanshi, P.Kaur, S.Dey, A.Srinivasan, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 57.30 / 1.82
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 68.314, 68.314, 108.418, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 20.7

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of Serine Proteinase K Complex with A Highly Flexible Hydrophobic Peptide at 1.8A Resolution (pdb code 2pq2). 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 Structure of Serine Proteinase K Complex with A Highly Flexible Hydrophobic Peptide at 1.8A Resolution, PDB code: 2pq2:

Calcium binding site 1 out of 1 in 2pq2

Go back to Calcium Binding Sites List in 2pq2
Calcium binding site 1 out of 1 in the Structure of Serine Proteinase K Complex with A Highly Flexible Hydrophobic Peptide at 1.8A Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Serine Proteinase K Complex with A Highly Flexible Hydrophobic Peptide at 1.8A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca500

b:12.6
occ:1.00
 O A:PRO175 2.3 13.4 1.0
O A:VAL177 2.4 13.1 1.0
OD2 A:ASP200 2.4 13.4 1.0
O A:HOH612 2.5 17.4 1.0
O A:HOH619 2.5 11.7 1.0
O A:HOH607 2.6 15.8 1.0
O A:HOH606 2.6 11.3 1.0
OD1 A:ASP200 2.7 14.4 1.0
CG A:ASP200 2.9 13.7 1.0
C A:PRO175 3.5 13.3 1.0
C A:VAL177 3.7 12.9 1.0
CA A:PRO175 4.1 13.4 1.0
N A:VAL177 4.2 13.3 1.0
O A:VAL198 4.3 14.9 1.0
CB A:ASP200 4.4 13.2 1.0
C A:SER176 4.5 13.3 1.0
N A:SER176 4.5 13.0 1.0
O A:GLU174 4.5 13.0 1.0
CA A:CYS178 4.6 12.3 1.0
N A:CYS178 4.6 12.6 1.0
CA A:VAL177 4.6 13.2 1.0
N A:THR179 4.7 12.2 1.0
O A:HOH676 4.7 31.5 1.0
O A:HOH856 4.7 46.4 1.0
O A:HOH652 4.7 23.6 1.0
O A:HOH857 4.7 32.0 1.0
CA A:SER176 4.7 13.2 1.0
OG1 A:THR179 4.8 12.7 1.0
O A:SER176 5.0 13.5 1.0
SG A:CYS249 5.0 13.6 1.0

Reference:

A.S.Ethayathulla, A.K.Singh, N.Singh, S.Sharma, M.Sinha, R.K.Somvanshi, P.Kaur, S.Dey, A.Srinivasan, T.P.Singh. Structure of Serine Proteinase K Complex with A Highly Flexible Hydrophobic Peptide at 1.8A Resolution To Be Published.
Page generated: Sat Dec 12 03:50:12 2020

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