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Calcium in PDB 1hn4: Prophospholipase A2 Dimer Complexed with MJ33, Sulfate, and Calcium

Enzymatic activity of Prophospholipase A2 Dimer Complexed with MJ33, Sulfate, and Calcium

All present enzymatic activity of Prophospholipase A2 Dimer Complexed with MJ33, Sulfate, and Calcium:
3.1.1.4;

Protein crystallography data

The structure of Prophospholipase A2 Dimer Complexed with MJ33, Sulfate, and Calcium, PDB code: 1hn4 was solved by T.M.Epstein, Y.H.Pan, M.K.Jain, B.J.Bahnson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 37.488, 54.852, 56.896, 90.00, 104.06, 90.00
R / Rfree (%) 21.5 / 23.9

Other elements in 1hn4:

The structure of Prophospholipase A2 Dimer Complexed with MJ33, Sulfate, and Calcium also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Prophospholipase A2 Dimer Complexed with MJ33, Sulfate, and Calcium (pdb code 1hn4). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Prophospholipase A2 Dimer Complexed with MJ33, Sulfate, and Calcium, PDB code: 1hn4:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1hn4

Go back to Calcium Binding Sites List in 1hn4
Calcium binding site 1 out of 2 in the Prophospholipase A2 Dimer Complexed with MJ33, Sulfate, and Calcium


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Prophospholipase A2 Dimer Complexed with MJ33, Sulfate, and Calcium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca290

b:2.3
occ:1.00
O A:TYR28 2.3 14.7 1.0
O A:GLY30 2.4 17.4 1.0
O22 A:MJI397 2.4 17.1 1.0
O A:GLY32 2.4 17.8 1.0
OD2 A:ASP49 2.4 14.9 1.0
O A:HOH408 2.5 21.3 1.0
CG A:ASP49 3.2 14.8 1.0
OD1 A:ASP49 3.3 14.7 1.0
C A:TYR28 3.5 14.7 1.0
C A:GLY32 3.5 17.9 1.0
C A:GLY30 3.5 17.5 1.0
N A:GLY32 3.6 18.7 1.0
P2 A:MJI397 3.8 16.9 1.0
N A:GLY30 3.8 15.8 1.0
O23 A:MJI397 4.0 16.8 1.0
CA A:GLY32 4.0 18.2 1.0
O A:HOH411 4.1 23.1 1.0
C A:LEU31 4.2 19.0 1.0
CA A:TYR28 4.2 14.7 1.0
C2 A:MJI397 4.4 20.8 1.0
CA A:GLY30 4.4 17.0 1.0
O A:HOH535 4.4 25.9 1.0
N A:LEU31 4.4 18.2 1.0
CA A:LEU31 4.4 18.8 1.0
N A:CYS29 4.5 14.6 1.0
O A:HOH466 4.5 27.5 1.0
CB A:TYR28 4.6 14.9 1.0
C A:CYS29 4.6 15.5 1.0
CA A:CYS29 4.6 15.0 1.0
O2 A:MJI397 4.6 18.9 1.0
N A:GLY33 4.6 17.6 1.0
CB A:ASP49 4.6 14.7 1.0
C31 A:MJI397 4.8 24.7 1.0
O A:CYS45 4.8 13.9 1.0
O21 A:MJI397 4.9 16.9 1.0
CA A:GLY33 5.0 17.5 1.0
CD1 A:TYR28 5.0 15.4 1.0
O A:LEU31 5.0 19.4 1.0
CB A:CYS45 5.0 13.6 1.0

Calcium binding site 2 out of 2 in 1hn4

Go back to Calcium Binding Sites List in 1hn4
Calcium binding site 2 out of 2 in the Prophospholipase A2 Dimer Complexed with MJ33, Sulfate, and Calcium


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Prophospholipase A2 Dimer Complexed with MJ33, Sulfate, and Calcium within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca291

b:13.5
occ:1.00
O B:TYR28 2.3 20.4 1.0
O B:GLY30 2.4 28.7 1.0
O B:GLY32 2.5 30.6 1.0
OD2 B:ASP49 2.5 20.2 1.0
O B:HOH525 2.6 28.2 1.0
OD1 B:ASP49 2.7 19.7 1.0
CG B:ASP49 2.9 18.9 1.0
C B:GLY32 3.4 30.3 1.0
C B:TYR28 3.4 20.5 1.0
C B:GLY30 3.5 28.2 1.0
N B:GLY32 3.6 30.6 1.0
N B:GLY30 3.6 24.8 1.0
O B:HOH509 3.8 35.8 1.0
CA B:GLY32 3.8 30.5 1.0
C B:LEU31 4.1 30.5 1.0
O B:HOH468 4.2 32.4 1.0
CA B:TYR28 4.2 20.3 1.0
CA B:GLY30 4.2 26.9 1.0
CB B:ASP49 4.3 18.2 1.0
N B:CYS29 4.4 21.0 1.0
N B:LEU31 4.4 29.4 1.0
C B:CYS29 4.4 23.1 1.0
O B:HOH469 4.5 35.9 1.0
CA B:CYS29 4.5 21.7 1.0
N B:GLY33 4.5 29.9 1.0
CA B:LEU31 4.6 30.3 1.0
CB B:TYR28 4.7 19.8 1.0
O B:LEU31 4.7 31.0 1.0
O B:CYS45 4.9 15.4 1.0

Reference:

T.M.Epstein, B.Z.Yu, Y.H.Pan, S.P.Tutton, B.P.Maliwal, M.K.Jain, B.J.Bahnson. The Basis For K(Cat) Impairment in Prophospholipase A(2) From the Anion-Assisted Dimer Structure. Biochemistry V. 40 11411 2001.
ISSN: ISSN 0006-2960
PubMed: 11560489
DOI: 10.1021/BI011228H
Page generated: Sat Dec 12 02:59:39 2020

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