Chlorine in PDB 3ju9: Crystal Structure of A Lectin From Canavalia Brasiliensis Seed (Conbr) Complexed with Alpha-Aminobutyric Acid

The structure of Crystal Structure of A Lectin From Canavalia Brasiliensis Seed (Conbr) Complexed with Alpha-Aminobutyric Acid, PDB code: 3ju9 was solved by E.H.S.Bezerra, B.A.M.Rocha, C.S.Nagano, G.A.Bezerra, T.R.Moura, M.J.B.Bezerra, R.G.Benevides, E.S.Marinho, P.Delatorre, B.S.Cavada, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.51 / 2.10
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	68.323, 73.020, 99.542, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 25.3

The structure of Crystal Structure of A Lectin From Canavalia Brasiliensis Seed (Conbr) Complexed with Alpha-Aminobutyric Acid also contains other interesting chemical elements:

Manganese	(Mn)	1 atom
Calcium	(Ca)	1 atom

The binding sites of Chlorine atom in the Crystal Structure of A Lectin From Canavalia Brasiliensis Seed (Conbr) Complexed with Alpha-Aminobutyric Acid (pdb code 3ju9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of A Lectin From Canavalia Brasiliensis Seed (Conbr) Complexed with Alpha-Aminobutyric Acid, PDB code: 3ju9:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of A Lectin From Canavalia Brasiliensis Seed (Conbr) Complexed with Alpha-Aminobutyric Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of A Lectin From Canavalia Brasiliensis Seed (Conbr) Complexed with Alpha-Aminobutyric Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl242 b:40.1 occ:1.00 N A:ALA236 3.6 35.3 1.0 CB A:ALA236 3.9 35.5 1.0 CA A:ASP235 4.0 35.8 1.0 NH2 A:ARG228 4.0 35.3 1.0 CB A:ASP235 4.1 36.0 1.0 C A:ASP235 4.2 35.8 1.0 CA A:ALA236 4.4 35.7 1.0 CD1 A:LEU229 4.9 28.4 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of A Lectin From Canavalia Brasiliensis Seed (Conbr) Complexed with Alpha-Aminobutyric Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of A Lectin From Canavalia Brasiliensis Seed (Conbr) Complexed with Alpha-Aminobutyric Acid within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl243 b:38.8 occ:1.00 O A:HOH382 2.2 36.7 1.0 ND2 A:ASN14 3.0 31.4 1.0 NH1 A:ARG228 3.4 35.5 1.0 OD1 A:ASP16 3.7 52.0 1.0 CB A:ASN14 3.8 34.3 1.0 CG A:ASN14 3.9 34.4 1.0 CD A:ARG228 4.0 32.1 1.0 CA A:ASN14 4.4 35.1 1.0 CZ A:ARG228 4.5 34.6 1.0 NE A:ARG228 4.6 34.4 1.0 O1 A:GOL239 4.7 33.5 1.0 CG A:ASP16 4.7 48.6 1.0 C1 A:GOL239 4.9 35.7 1.0 OD2 A:ASP16 5.0 50.6 1.0

E.H.Bezerra, B.A.Rocha, C.S.Nagano, G.A.Bezerra, T.R.Moura, M.J.Bezerra, R.G.Benevides, A.H.Sampaio, A.M.Assreuy, P.Delatorre, B.S.Cavada. Structural Analysis of Conbr Reveals Molecular Correlation Between the Carbohydrate Recognition Domain and Endothelial No Synthase Activation. Biochem.Biophys.Res.Commun. V. 408 566 2011.
ISSN: ISSN 0006-291X
PubMed: 21530490
DOI: 10.1016/J.BBRC.2011.04.061