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Chlorine in PDB 4ate: High Resolution Crystal Structure of Beta-Porphyranase A From Zobellia Galactanivorans

Enzymatic activity of High Resolution Crystal Structure of Beta-Porphyranase A From Zobellia Galactanivorans

All present enzymatic activity of High Resolution Crystal Structure of Beta-Porphyranase A From Zobellia Galactanivorans:
3.2.1.178;

Protein crystallography data

The structure of High Resolution Crystal Structure of Beta-Porphyranase A From Zobellia Galactanivorans, PDB code: 4ate was solved by J.H.Hehemann, G.Correc, M.Jam, G.Michel, M.Czjzek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.86 / 1.10
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 70.270, 70.270, 92.470, 90.00, 90.00, 120.00
R / Rfree (%) 12.4 / 15.2

Other elements in 4ate:

The structure of High Resolution Crystal Structure of Beta-Porphyranase A From Zobellia Galactanivorans also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the High Resolution Crystal Structure of Beta-Porphyranase A From Zobellia Galactanivorans (pdb code 4ate). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the High Resolution Crystal Structure of Beta-Porphyranase A From Zobellia Galactanivorans, PDB code: 4ate:

Chlorine binding site 1 out of 1 in 4ate

Go back to Chlorine Binding Sites List in 4ate
Chlorine binding site 1 out of 1 in the High Resolution Crystal Structure of Beta-Porphyranase A From Zobellia Galactanivorans


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of High Resolution Crystal Structure of Beta-Porphyranase A From Zobellia Galactanivorans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1277

b:7.5
occ:1.00
 N A:LYS250 3.2 6.6 1.0
O A:HOH2279 3.2 8.7 1.0
N A:SER125 3.2 5.4 1.0
ND2 A:ASN253 3.2 9.0 1.0
CA A:PRO249 3.6 5.3 1.0
CA A:LEU124 3.7 6.0 1.0
CB A:ASN253 3.8 6.9 1.0
CB A:PRO249 3.8 5.6 1.0
C A:PRO249 3.9 5.6 1.0
C A:LEU124 3.9 5.2 1.0
CG A:ASN253 4.0 8.8 1.0
CB A:LYS250 4.0 8.2 1.0
CD2 A:LEU124 4.0 8.9 1.0
CB A:SER125 4.0 5.4 1.0
CG A:LYS250 4.1 10.8 1.0
CA A:LYS250 4.1 6.6 1.0
CB A:LEU124 4.2 6.1 1.0
CA A:SER125 4.2 5.3 1.0
O A:LYS250 4.3 7.0 1.0
O A:SER123 4.4 9.3 1.0
O A:ASN148 4.5 6.5 1.0
ND2 A:ASN148 4.6 12.8 1.0
CD A:LYS250 4.7 18.6 1.0
C A:LYS250 4.7 6.4 1.0
CG A:LEU124 4.8 6.1 1.0
N A:LEU124 4.8 6.5 1.0
N A:PRO249 4.9 5.3 1.0

Reference:

J.H.Hehemann, G.Correc, F.Thomas, T.Bernard, T.Barbeyron, M.Jam, W.Helbert, G.Michel, M.Czjzek. Biochemical and Structural Characterization of the Complex Agarolytic Enzyme System From the Marine Bacterium Zobellia Galactanivorans. J.Biol.Chem. V. 287 30571 2012.
ISSN: ISSN 0021-9258
PubMed: 22778272
DOI: 10.1074/JBC.M112.377184
Page generated: Sat Dec 12 10:24:33 2020

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