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Calcium in PDB 1oyo: Regulation of Protease Activity By Melanin: Crystal Structure of the Complex Formed Between Proteinase K and Melanin Monomers at 2.0 Resolution

Enzymatic activity of Regulation of Protease Activity By Melanin: Crystal Structure of the Complex Formed Between Proteinase K and Melanin Monomers at 2.0 Resolution

All present enzymatic activity of Regulation of Protease Activity By Melanin: Crystal Structure of the Complex Formed Between Proteinase K and Melanin Monomers at 2.0 Resolution:
3.4.21.64;

Protein crystallography data

The structure of Regulation of Protease Activity By Melanin: Crystal Structure of the Complex Formed Between Proteinase K and Melanin Monomers at 2.0 Resolution, PDB code: 1oyo was solved by N.Singh, S.Sharma, S.Kumar, G.Raman, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.71 / 2.02
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 68.319, 68.319, 108.292, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / 19

Calcium Binding Sites:

The binding sites of Calcium atom in the Regulation of Protease Activity By Melanin: Crystal Structure of the Complex Formed Between Proteinase K and Melanin Monomers at 2.0 Resolution (pdb code 1oyo). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Regulation of Protease Activity By Melanin: Crystal Structure of the Complex Formed Between Proteinase K and Melanin Monomers at 2.0 Resolution, PDB code: 1oyo:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1oyo

Go back to Calcium Binding Sites List in 1oyo
Calcium binding site 1 out of 2 in the Regulation of Protease Activity By Melanin: Crystal Structure of the Complex Formed Between Proteinase K and Melanin Monomers at 2.0 Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Regulation of Protease Activity By Melanin: Crystal Structure of the Complex Formed Between Proteinase K and Melanin Monomers at 2.0 Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1001

b:17.9
occ:1.00
 O A:VAL177 2.5 15.5 1.0
O A:PRO175 2.5 12.9 1.0
OD1 A:ASP200 2.6 10.8 1.0
O A:HOH1004 2.7 20.2 1.0
O A:HOH1005 2.7 12.8 1.0
O A:HOH1006 2.7 12.9 1.0
OD2 A:ASP200 2.7 14.2 1.0
O A:HOH1003 2.7 18.7 1.0
CG A:ASP200 3.0 15.1 1.0
C A:PRO175 3.6 14.7 1.0
C A:VAL177 3.7 14.9 1.0
CA A:PRO175 4.2 15.3 1.0
N A:VAL177 4.2 15.6 1.0
O A:VAL198 4.3 16.2 1.0
O A:HOH1078 4.4 49.7 1.0
CB A:ASP200 4.4 12.7 1.0
C A:SER176 4.5 15.4 1.0
O A:GLU174 4.5 14.0 1.0
CA A:CYS178 4.5 12.5 1.0
O A:HOH1101 4.5 35.1 1.0
N A:SER176 4.6 12.4 1.0
N A:CYS178 4.6 13.3 1.0
N A:THR179 4.6 11.0 1.0
CA A:VAL177 4.6 14.2 1.0
O A:HOH1010 4.8 21.8 1.0
CA A:SER176 4.8 15.2 1.0
OG1 A:THR179 4.8 12.5 1.0
SG A:CYS249 4.9 12.8 1.0
O A:SER176 5.0 15.1 1.0

Calcium binding site 2 out of 2 in 1oyo

Go back to Calcium Binding Sites List in 1oyo
Calcium binding site 2 out of 2 in the Regulation of Protease Activity By Melanin: Crystal Structure of the Complex Formed Between Proteinase K and Melanin Monomers at 2.0 Resolution


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Regulation of Protease Activity By Melanin: Crystal Structure of the Complex Formed Between Proteinase K and Melanin Monomers at 2.0 Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1002

b:82.9
occ:0.40
 O A:THR16 3.1 26.1 1.0
O A:HOH1007 3.4 41.9 1.0
OD2 A:ASP260 3.6 31.0 1.0
OD1 A:ASP260 3.9 36.2 1.0
O A:HOH1008 3.9 81.2 1.0
CG A:ASP260 4.1 30.2 1.0
C A:THR16 4.3 24.7 1.0
CG2 A:THR16 4.5 25.1 1.0
OG1 A:THR16 4.7 29.8 1.0
CB A:THR16 5.0 26.5 1.0

Reference:

N.Singh, S.Sharma, S.Kumar, G.Raman, T.P.Singh. Regulation of Protease Activity By Melanin: Crystal Structure of the Complex Formed Between Proteinase K and Melanin Monomers at 2.0 Resolution To Be Published.
Page generated: Sat Dec 12 03:13:22 2020

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