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Calcium in PDB 3njv: Rhamnogalacturonan Lyase From Aspergillus Aculeatus K150A Substrate Complex

Enzymatic activity of Rhamnogalacturonan Lyase From Aspergillus Aculeatus K150A Substrate Complex

All present enzymatic activity of Rhamnogalacturonan Lyase From Aspergillus Aculeatus K150A Substrate Complex:
4.2.2.10;

Protein crystallography data

The structure of Rhamnogalacturonan Lyase From Aspergillus Aculeatus K150A Substrate Complex, PDB code: 3njv 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) 20.00 / 2.40
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 76.974, 76.974, 170.649, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 25.2

Calcium Binding Sites:

The binding sites of Calcium atom in the Rhamnogalacturonan Lyase From Aspergillus Aculeatus K150A Substrate Complex (pdb code 3njv). 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 K150A Substrate Complex, PDB code: 3njv:

Calcium binding site 1 out of 1 in 3njv

Go back to Calcium Binding Sites List in 3njv
Calcium binding site 1 out of 1 in the Rhamnogalacturonan Lyase From Aspergillus Aculeatus K150A Substrate Complex


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 K150A Substrate Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca800

b:20.2
occ:1.00
O A:GLN351 2.3 6.7 1.0
OD1 A:ASP349 2.4 8.5 1.0
O A:HOH606 2.4 15.6 1.0
O A:ASP502 2.4 5.1 1.0
O A:GLU347 2.4 7.2 1.0
OD2 A:ASP502 2.5 6.3 1.0
C A:ASP502 3.2 5.6 1.0
CG A:ASP349 3.4 8.2 1.0
C A:GLN351 3.5 7.0 1.0
C A:GLU347 3.6 7.4 1.0
CG A:ASP502 3.6 5.5 1.0
CA A:ASP502 3.7 5.8 1.0
N A:GLN351 3.8 6.6 1.0
N A:GLU347 3.9 7.8 1.0
OD2 A:ASP349 3.9 10.8 1.0
N A:ASP349 3.9 7.2 1.0
CA A:GLN351 4.2 7.1 1.0
CA A:GLU347 4.3 7.8 1.0
CB A:ASP502 4.3 5.9 1.0
N A:GLY350 4.3 6.6 1.0
N A:CYS503 4.3 5.9 1.0
CE2 A:PHE355 4.3 11.0 1.0
CB A:ASP349 4.5 7.2 1.0
N A:THR353 4.5 8.6 1.0
CA A:ASP349 4.6 7.2 1.0
N A:PRO352 4.6 7.3 1.0
OD1 A:ASP502 4.6 6.2 1.0
N A:TRP348 4.6 7.2 1.0
C A:ASP349 4.6 6.7 1.0
CB A:CYS503 4.7 6.2 1.0
CA A:PRO352 4.8 7.7 1.0
CB A:GLN351 4.8 7.1 1.0
CA A:CYS503 4.8 6.2 1.0
O A:THR353 4.8 9.4 1.0
CB A:GLU347 4.8 8.1 1.0
CA A:TRP348 4.8 6.9 1.0
C A:GLY350 4.9 6.5 1.0
C A:PRO352 4.9 8.1 1.0
C A:TRP348 4.9 7.2 1.0
C A:GLY346 4.9 7.8 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 15:01:28 2024

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