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Calcium in PDB 3njx: Rhamnogalacturonan Lyase From Aspergillus Aculeatus Mutant H210A

Enzymatic activity of Rhamnogalacturonan Lyase From Aspergillus Aculeatus Mutant H210A

All present enzymatic activity of Rhamnogalacturonan Lyase From Aspergillus Aculeatus Mutant H210A:
4.2.2.10;

Protein crystallography data

The structure of Rhamnogalacturonan Lyase From Aspergillus Aculeatus Mutant H210A, PDB code: 3njx was solved by M.H.Jensen, H.Otten, U.Christensen, T.V.Borchert, L.L.H.Christensen, S.Larsen, L.Lo Leggio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.94 / 1.94
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 77.071, 77.071, 171.099, 90.00, 90.00, 90.00
R / Rfree (%) 16.7 / 20

Calcium Binding Sites:

The binding sites of Calcium atom in the Rhamnogalacturonan Lyase From Aspergillus Aculeatus Mutant H210A (pdb code 3njx). 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 Rhamnogalacturonan Lyase From Aspergillus Aculeatus Mutant H210A, PDB code: 3njx:

Calcium binding site 1 out of 1 in 3njx

Go back to Calcium Binding Sites List in 3njx
Calcium binding site 1 out of 1 in the Rhamnogalacturonan Lyase From Aspergillus Aculeatus Mutant H210A


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Rhamnogalacturonan Lyase From Aspergillus Aculeatus Mutant H210A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca800

b:21.6
occ:1.00
OD1 A:ASP349 2.3 9.8 1.0
O A:GLN351 2.3 10.2 1.0
O A:HOH848 2.4 16.6 1.0
O A:ASP502 2.4 8.4 1.0
O A:GLU347 2.4 10.2 1.0
OD2 A:ASP502 2.5 8.7 1.0
C A:ASP502 3.3 8.6 1.0
CG A:ASP349 3.3 10.6 1.0
C A:GLN351 3.5 10.5 1.0
C A:GLU347 3.6 10.6 1.0
CG A:ASP502 3.7 8.8 1.0
CA A:ASP502 3.7 8.6 1.0
OD2 A:ASP349 3.8 11.4 1.0
N A:GLN351 3.9 10.4 1.0
N A:GLU347 3.9 10.6 1.0
N A:ASP349 3.9 10.3 1.0
CA A:GLN351 4.2 10.6 1.0
CB A:ASP502 4.3 8.4 1.0
CA A:GLU347 4.3 11.0 1.0
CE2 A:PHE355 4.4 13.7 1.0
N A:CYS503 4.4 8.9 1.0
N A:GLY350 4.4 10.2 1.0
N A:THR353 4.5 11.2 1.0
CB A:ASP349 4.5 10.3 1.0
N A:PRO352 4.5 10.5 1.0
CA A:ASP349 4.6 10.2 1.0
N A:TRP348 4.6 10.5 1.0
CA A:PRO352 4.6 10.7 1.0
OD1 A:ASP502 4.7 9.2 1.0
C A:ASP349 4.7 10.2 1.0
CB A:CYS503 4.7 9.1 1.0
CB A:GLN351 4.8 10.6 1.0
O A:THR353 4.8 11.3 1.0
CB A:GLU347 4.8 11.3 1.0
CA A:TRP348 4.8 10.4 1.0
CA A:CYS503 4.9 9.0 1.0
C A:PRO352 4.9 11.0 1.0
C A:TRP348 4.9 10.4 1.0
C A:GLY350 5.0 10.5 1.0
C A:GLY346 5.0 10.7 1.0

Reference:

M.H.Jensen, H.Otten, U.Christensen, T.V.Borchert, L.L.Christensen, S.Larsen, L.L.Leggio. Structural and Biochemical Studies Elucidate the Mechanism of Rhamnogalacturonan Lyase From Aspergillus Aculeatus. J.Mol.Biol. V. 404 100 2010.
ISSN: ISSN 0022-2836
PubMed: 20851126
DOI: 10.1016/J.JMB.2010.09.013
Page generated: Sat Jul 13 15:01:47 2024

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