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Calcium in PDB 1pa2: Arabidopsis Thaliana Peroxidase A2

Enzymatic activity of Arabidopsis Thaliana Peroxidase A2

All present enzymatic activity of Arabidopsis Thaliana Peroxidase A2:
1.11.1.7;

Protein crystallography data

The structure of Arabidopsis Thaliana Peroxidase A2, PDB code: 1pa2 was solved by A.Henriksen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 99.00 / 1.45
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.156, 74.597, 80.446, 90.00, 90.00, 90.00
R / Rfree (%) 14.8 / 18.9

Other elements in 1pa2:

The structure of Arabidopsis Thaliana Peroxidase A2 also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Iron (Fe) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Arabidopsis Thaliana Peroxidase A2 (pdb code 1pa2). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Arabidopsis Thaliana Peroxidase A2, PDB code: 1pa2:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 1pa2

Go back to Calcium Binding Sites List in 1pa2
Calcium binding site 1 out of 2 in the Arabidopsis Thaliana Peroxidase A2


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Arabidopsis Thaliana Peroxidase A2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca307

b:3.7
occ:1.00
O A:VAL46 2.2 4.5 1.0
OD1 A:ASP43 2.3 5.0 1.0
OD1 A:ASP50 2.4 3.7 1.0
O A:ASP43 2.4 4.1 1.0
O A:HOH591 2.4 5.2 1.0
OG A:SER52 2.5 4.5 1.0
O A:GLY48 2.5 4.5 1.0
C A:ASP43 3.3 4.9 1.0
C A:VAL46 3.5 4.7 1.0
CG A:ASP43 3.5 6.2 1.0
CG A:ASP50 3.5 5.2 1.0
CB A:SER52 3.6 3.9 1.0
CA A:ASP43 3.7 4.8 1.0
C A:GLY48 3.7 5.6 1.0
N A:SER52 3.9 3.4 1.0
N A:ASP50 4.0 3.1 1.0
OD2 A:ASP50 4.1 4.6 1.0
CB A:ASP43 4.2 4.7 1.0
C A:ASN47 4.2 4.0 1.0
CA A:VAL46 4.3 5.5 1.0
CA A:SER52 4.3 2.5 1.0
N A:GLY48 4.3 4.3 1.0
O A:ASN47 4.3 6.1 1.0
N A:VAL46 4.4 4.0 1.0
CB A:VAL46 4.4 6.6 1.0
OD2 A:ASP43 4.4 4.9 1.0
N A:CYS44 4.4 3.9 1.0
N A:ASN47 4.4 5.3 1.0
CB A:ASN47 4.5 6.3 1.0
N A:ALA51 4.5 3.3 1.0
N A:ILE53 4.6 4.7 1.0
CB A:ASP50 4.6 2.9 1.0
CA A:ASN47 4.6 4.7 1.0
CA A:GLY48 4.6 5.3 1.0
N A:CYS49 4.7 3.9 1.0
O A:HIS42 4.7 5.6 1.0
OE2 A:GLU64 4.7 4.8 1.0
OE1 A:GLU64 4.7 6.5 1.0
CA A:ASP50 4.7 2.9 1.0
CA A:CYS49 4.8 4.0 1.0
C A:ASP50 4.8 2.7 1.0
CA A:CYS44 4.9 4.2 1.0
C A:SER52 4.9 5.2 1.0
C A:CYS49 4.9 6.2 1.0
C A:ALA51 5.0 2.4 1.0

Calcium binding site 2 out of 2 in 1pa2

Go back to Calcium Binding Sites List in 1pa2
Calcium binding site 2 out of 2 in the Arabidopsis Thaliana Peroxidase A2


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Arabidopsis Thaliana Peroxidase A2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca308

b:4.2
occ:1.00
OD2 A:ASP221 2.3 7.0 1.0
O A:THR170 2.4 4.2 1.0
O A:ALA227 2.4 6.9 1.0
OG1 A:THR224 2.4 7.2 1.0
O A:THR224 2.4 5.9 1.0
OD1 A:ASP229 2.5 5.5 1.0
OG1 A:THR170 2.5 4.9 1.0
C A:THR170 3.4 4.8 1.0
CG A:ASP221 3.4 6.2 1.0
CG A:ASP229 3.4 6.7 1.0
C A:THR224 3.5 6.8 1.0
CB A:THR224 3.5 7.2 1.0
C A:ALA227 3.5 4.1 1.0
CB A:THR170 3.6 4.4 1.0
OD2 A:ASP229 3.8 7.0 1.0
CA A:THR170 3.8 4.5 1.0
CA A:THR224 3.9 6.5 1.0
CB A:ASP221 4.0 4.1 1.0
CG2 A:THR170 4.2 3.6 1.0
N A:ALA227 4.2 5.5 1.0
N A:THR224 4.3 5.0 1.0
CA A:ALA227 4.3 3.2 1.0
N A:ASP229 4.3 6.5 1.0
OD1 A:ASP221 4.4 6.5 1.0
CB A:ALA227 4.5 6.9 1.0
N A:PHE171 4.5 3.6 1.0
CB A:ASN231 4.5 6.0 1.0
N A:PHE228 4.6 3.3 1.0
N A:PRO225 4.6 4.7 1.0
O A:ASP229 4.6 4.8 1.0
CB A:ASP229 4.7 6.0 1.0
CA A:PHE228 4.8 5.1 1.0
CG2 A:THR224 4.8 7.1 1.0
C A:PRO225 4.9 6.4 1.0
CA A:ASP229 4.9 4.2 1.0
C A:PHE228 4.9 5.4 1.0
CG A:ASN231 5.0 5.6 1.0
CA A:PHE171 5.0 4.3 1.0

Reference:

L.Ostergaard, K.Teilum, O.Mirza, O.Mattsson, M.Petersen, K.G.Welinder, J.Mundy, M.Gajhede, A.Henriksen. Arabidopsis Atp A2 Peroxidase. Expression and High-Resolution Structure of A Plant Peroxidase with Implications For Lignification. Plant Mol.Biol. V. 44 231 2000.
ISSN: ISSN 0167-4412
PubMed: 11117266
DOI: 10.1023/A:1006442618860
Page generated: Thu Jul 11 13:41:11 2024

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