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Calcium in PDB 1c74: Structure of the Double Mutant (K53,56M) of Phospholipase A2

Enzymatic activity of Structure of the Double Mutant (K53,56M) of Phospholipase A2

All present enzymatic activity of Structure of the Double Mutant (K53,56M) of Phospholipase A2:
3.1.1.4;

Protein crystallography data

The structure of Structure of the Double Mutant (K53,56M) of Phospholipase A2, PDB code: 1c74 was solved by K.Sekar, M.D.Tsai, M.K.Jain, S.Ramakumar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.90
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 46.410, 46.410, 102.720, 90.00, 90.00, 120.00
R / Rfree (%) 18.9 / 22.4

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure of the Double Mutant (K53,56M) of Phospholipase A2 (pdb code 1c74). 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 Structure of the Double Mutant (K53,56M) of Phospholipase A2, PDB code: 1c74:

Calcium binding site 1 out of 1 in 1c74

Go back to Calcium Binding Sites List in 1c74
Calcium binding site 1 out of 1 in the Structure of the Double Mutant (K53,56M) of Phospholipase A2


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of the Double Mutant (K53,56M) of Phospholipase A2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca124

b:16.9
occ:1.00
O A:TYR28 2.2 15.8 1.0
O A:HOH202 2.3 11.6 1.0
O A:GLY30 2.3 22.7 1.0
O A:GLY32 2.4 21.9 1.0
OD2 A:ASP49 2.4 15.0 1.0
O A:HOH203 2.5 31.2 1.0
OD1 A:ASP49 2.6 16.6 1.0
CG A:ASP49 2.9 16.8 1.0
C A:TYR28 3.4 15.7 1.0
C A:GLY30 3.6 22.5 1.0
C A:GLY32 3.6 25.5 1.0
N A:GLY30 3.8 17.7 1.0
N A:GLY32 4.0 28.0 1.0
O A:HOH205 4.1 15.7 1.0
CA A:TYR28 4.2 16.4 1.0
C A:LEU31 4.3 28.7 1.0
CA A:GLY32 4.4 25.8 1.0
O A:HOH223 4.4 20.1 1.0
CB A:ASP49 4.4 13.6 1.0
CA A:GLY30 4.4 20.8 1.0
N A:CYS29 4.4 15.6 1.0
N A:LEU31 4.5 25.2 1.0
CA A:LEU31 4.5 28.7 1.0
CA A:CYS29 4.6 16.4 1.0
N A:GLY33 4.6 24.9 1.0
CB A:TYR28 4.7 15.2 1.0
C A:CYS29 4.7 18.4 1.0
O A:LEU31 4.8 30.6 1.0
CA A:GLY33 4.8 24.2 1.0
O A:HOH231 4.8 33.6 1.0
O A:CYS45 4.8 10.2 1.0

Reference:

B.Z.Yu, M.J.Poi, U.A.Ramagopal, R.Jain, S.Ramakumar, O.G.Berg, M.D.Tsai, K.Sekar, M.K.Jain. Structural Basis of the Anionic Interface Preference and K*Cat Activation of Pancreatic Phospholipase A2. Biochemistry V. 39 12312 2000.
ISSN: ISSN 0006-2960
PubMed: 11015210
DOI: 10.1021/BI000740K
Page generated: Thu Jul 11 06:52:12 2024

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