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Calcium in PDB 1okg: 3-Mercaptopyruvate Sulfurtransferase From Leishmania Major

Enzymatic activity of 3-Mercaptopyruvate Sulfurtransferase From Leishmania Major

All present enzymatic activity of 3-Mercaptopyruvate Sulfurtransferase From Leishmania Major:
2.8.1.2;

Protein crystallography data

The structure of 3-Mercaptopyruvate Sulfurtransferase From Leishmania Major, PDB code: 1okg was solved by M.S.Alphey, W.N.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 76.70 / 2.10
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 109.574, 109.574, 67.300, 90.00, 90.00, 90.00
R / Rfree (%) 20.8 / 28.7

Other elements in 1okg:

The structure of 3-Mercaptopyruvate Sulfurtransferase From Leishmania Major also contains other interesting chemical elements:

Arsenic (As) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the 3-Mercaptopyruvate Sulfurtransferase From Leishmania Major (pdb code 1okg). 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 3-Mercaptopyruvate Sulfurtransferase From Leishmania Major, PDB code: 1okg:

Calcium binding site 1 out of 1 in 1okg

Go back to Calcium Binding Sites List in 1okg
Calcium binding site 1 out of 1 in the 3-Mercaptopyruvate Sulfurtransferase From Leishmania Major


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of 3-Mercaptopyruvate Sulfurtransferase From Leishmania Major within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1373

b:66.2
occ:0.50
CG A:ASP299 4.2 35.9 1.0
CB A:ASP299 4.3 34.1 1.0
OD2 A:ASP299 4.3 37.0 1.0
OH A:TYR300 4.6 38.7 1.0
OD1 A:ASP299 4.6 34.4 1.0
CE2 A:TYR300 4.7 34.4 1.0
CZ A:TYR300 4.8 35.8 1.0
CA A:ASP299 5.0 33.4 1.0
O A:ASP299 5.0 33.1 1.0

Reference:

M.S.Alphey, R.A.M.Williams, J.C.Mottram, G.H.Coombs, W.N.Hunter. The Crystal Structure of Leishmania Major 3-Mercaptopyruvate Sulfurtransferase: A Three-Domain Architecture with A Serine Protease-Like Triad at the Active Site J.Biol.Chem. V. 278 48219 2003.
ISSN: ISSN 0021-9258
PubMed: 12952945
DOI: 10.1074/JBC.M307187200
Page generated: Sat Dec 12 03:12:33 2020

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