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Calcium in PDB 1cnm: Enhancement of Catalytic Efficiency of Proteinase K Through Exposure to Anhydrous Organic Solvent at 70 Degrees Celsius

Enzymatic activity of Enhancement of Catalytic Efficiency of Proteinase K Through Exposure to Anhydrous Organic Solvent at 70 Degrees Celsius

All present enzymatic activity of Enhancement of Catalytic Efficiency of Proteinase K Through Exposure to Anhydrous Organic Solvent at 70 Degrees Celsius:
3.4.21.64;

Protein crystallography data

The structure of Enhancement of Catalytic Efficiency of Proteinase K Through Exposure to Anhydrous Organic Solvent at 70 Degrees Celsius, PDB code: 1cnm was solved by M.N.Gupta, R.Tyagi, S.Sharma, S.Karthikeyan, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.20
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 68.320, 68.320, 108.370, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Enhancement of Catalytic Efficiency of Proteinase K Through Exposure to Anhydrous Organic Solvent at 70 Degrees Celsius (pdb code 1cnm). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Enhancement of Catalytic Efficiency of Proteinase K Through Exposure to Anhydrous Organic Solvent at 70 Degrees Celsius, PDB code: 1cnm:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1cnm

Go back to Calcium Binding Sites List in 1cnm
Calcium binding site 1 out of 2 in the Enhancement of Catalytic Efficiency of Proteinase K Through Exposure to Anhydrous Organic Solvent at 70 Degrees Celsius


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Enhancement of Catalytic Efficiency of Proteinase K Through Exposure to Anhydrous Organic Solvent at 70 Degrees Celsius within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca280

b:16.7
occ:1.00
O A:PRO175 2.7 10.9 1.0
O A:VAL177 2.7 12.2 1.0
OD2 A:ASP200 2.8 11.4 1.0
O A:HOH504 2.8 8.8 1.0
O A:HOH502 2.8 16.0 1.0
O A:HOH501 2.9 13.6 1.0
O A:HOH503 2.9 18.4 1.0
OD1 A:ASP200 3.0 12.2 1.0
CG A:ASP200 3.2 11.8 1.0
C A:PRO175 3.7 11.1 1.0
C A:VAL177 4.0 11.6 1.0
CA A:PRO175 4.1 11.2 1.0
O A:VAL198 4.2 12.9 1.0
O A:HOH581 4.3 44.8 1.0
N A:VAL177 4.3 11.3 1.0
O A:GLU174 4.5 10.2 1.0
C A:SER176 4.5 11.5 1.0
CA A:CYS178 4.6 10.5 1.0
N A:THR179 4.6 9.5 1.0
N A:SER176 4.7 10.9 1.0
CB A:ASP200 4.7 11.3 1.0
O A:HOH605 4.7 34.1 1.0
N A:CYS178 4.7 11.2 1.0
CA A:VAL177 4.8 11.2 1.0
OG1 A:THR179 4.8 8.2 1.0
CA A:SER176 4.8 11.3 1.0
O A:HOH509 4.9 14.9 1.0
O A:SER176 4.9 11.6 1.0

Calcium binding site 2 out of 2 in 1cnm

Go back to Calcium Binding Sites List in 1cnm
Calcium binding site 2 out of 2 in the Enhancement of Catalytic Efficiency of Proteinase K Through Exposure to Anhydrous Organic Solvent at 70 Degrees Celsius


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Enhancement of Catalytic Efficiency of Proteinase K Through Exposure to Anhydrous Organic Solvent at 70 Degrees Celsius within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca281

b:17.9
occ:0.40
O A:THR16 2.9 19.2 1.0
OD1 A:ASP260 3.0 26.2 1.0
O A:HOH506 3.1 56.2 1.0
O A:HOH505 3.1 28.2 1.0
OD2 A:ASP260 3.2 26.4 1.0
CG A:ASP260 3.4 25.8 1.0
C A:THR16 3.9 19.3 1.0
OG1 A:THR16 4.7 19.7 1.0
CA A:THR16 4.8 19.0 1.0
CG2 A:THR16 4.8 19.3 1.0
N A:SER17 4.8 19.5 1.0
ND2 A:ASN257 4.9 16.8 1.0
CB A:ASP260 4.9 24.7 1.0
CA A:SER17 4.9 19.3 1.0
CB A:THR16 5.0 19.4 1.0

Reference:

M.N.Gupta, R.Tyagi, S.Sharma, S.Karthikeyan, T.P.Singh. Enhancement of Catalytic Efficiency of Enzymes Through Exposure to Anhydrous Organic Solvent at 70 Degrees C. Three-Dimensional Structure of A Treated Serine Proteinase at 2.2 A Resolution. Proteins V. 39 226 2000.
ISSN: ISSN 0887-3585
PubMed: 10737944
DOI: 10.1002/(SICI)1097-0134(20000515)39:3<226::AID-PROT50>3.0.CO;2-Y
Page generated: Sat Dec 12 02:51:49 2020

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