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Calcium in PDB 2bpp: Phospholipase A2 Engineering. X-Ray Structural and Functional Evidence For the Interaction of Lysine-56 with Substrates

Enzymatic activity of Phospholipase A2 Engineering. X-Ray Structural and Functional Evidence For the Interaction of Lysine-56 with Substrates

All present enzymatic activity of Phospholipase A2 Engineering. X-Ray Structural and Functional Evidence For the Interaction of Lysine-56 with Substrates:
3.1.1.4;

Protein crystallography data

The structure of Phospholipase A2 Engineering. X-Ray Structural and Functional Evidence For the Interaction of Lysine-56 with Substrates, PDB code: 2bpp was solved by M.Sundaralingam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.80
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 46.520, 46.520, 102.200, 90.00, 90.00, 120.00
R / Rfree (%) 18.8 / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Phospholipase A2 Engineering. X-Ray Structural and Functional Evidence For the Interaction of Lysine-56 with Substrates (pdb code 2bpp). 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 Phospholipase A2 Engineering. X-Ray Structural and Functional Evidence For the Interaction of Lysine-56 with Substrates, PDB code: 2bpp:

Calcium binding site 1 out of 1 in 2bpp

Go back to Calcium Binding Sites List in 2bpp
Calcium binding site 1 out of 1 in the Phospholipase A2 Engineering. X-Ray Structural and Functional Evidence For the Interaction of Lysine-56 with Substrates


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Phospholipase A2 Engineering. X-Ray Structural and Functional Evidence For the Interaction of Lysine-56 with Substrates within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca124

b:14.6
occ:1.00
 O A:TYR28 1.9 13.6 1.0
O A:GLY32 2.0 22.3 1.0
OD2 A:ASP49 2.2 12.4 1.0
O A:GLY30 2.4 18.6 1.0
OD1 A:ASP49 2.4 9.6 1.0
CG A:ASP49 2.7 11.7 1.0
C A:TYR28 3.1 13.8 1.0
C A:GLY32 3.2 24.2 1.0
C A:GLY30 3.6 18.9 1.0
N A:GLY30 3.8 15.7 1.0
CA A:TYR28 3.9 12.9 1.0
N A:GLY32 4.0 22.3 1.0
CA A:GLY32 4.0 24.3 1.0
N A:CYS29 4.2 14.2 1.0
CB A:ASP49 4.2 11.0 1.0
N A:GLY33 4.3 24.0 1.0
CA A:GLY30 4.4 16.8 1.0
C A:LEU31 4.4 24.1 1.0
CB A:TYR28 4.5 11.0 1.0
CA A:CYS29 4.5 14.7 1.0
C A:CYS29 4.6 14.7 1.0
CA A:GLY33 4.6 23.9 1.0
N A:LEU31 4.6 20.9 1.0
O A:CYS45 4.8 10.7 1.0
O A:LEU31 4.8 27.2 1.0
CA A:LEU31 4.9 23.5 1.0
CD1 A:TYR28 5.0 12.5 1.0

Reference:

J.P.Noel, C.A.Bingman, T.L.Deng, C.M.Dupureur, K.J.Hamilton, R.T.Jiang, J.G.Kwak, C.Sekharudu, M.Sundaralingam, M.D.Tsai. Phospholipase A2 Engineering. X-Ray Structural and Functional Evidence For the Interaction of Lysine-56 with Substrates. Biochemistry V. 30 11801 1991.
ISSN: ISSN 0006-2960
PubMed: 1751497
DOI: 10.1021/BI00115A010
Page generated: Fri Jul 12 09:08:22 2024

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