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

Protein crystallography data

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

Other elements in 3ju9:

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
Chlorine (Cl) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium 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 Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of A Lectin From Canavalia Brasiliensis Seed (Conbr) Complexed with Alpha-Aminobutyric Acid, PDB code: 3ju9:

Calcium binding site 1 out of 1 in 3ju9

Go back to Calcium Binding Sites List in 3ju9
Calcium binding site 1 out of 1 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 Calcium with other atoms in the Ca 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:Ca240

b:29.0
occ:1.00
O A:TYR12 2.3 28.5 1.0
O A:HOH244 2.3 20.6 1.0
O A:HOH245 2.3 24.1 1.0
OD2 A:ASP19 2.4 33.6 1.0
OD1 A:ASN14 2.4 30.3 1.0
OD1 A:ASP10 2.5 25.6 1.0
OD2 A:ASP10 2.7 24.2 1.0
CG A:ASP10 3.0 24.8 1.0
CG A:ASP19 3.5 34.9 1.0
CG A:ASN14 3.6 34.4 1.0
C A:TYR12 3.6 28.6 1.0
N A:ASN14 3.9 32.8 1.0
OD1 A:ASP19 4.0 32.0 1.0
CB A:ASN14 4.2 34.3 1.0
MN A:MN241 4.2 25.4 1.0
CA A:TYR12 4.5 28.4 1.0
CA A:PRO13 4.5 30.0 1.0
CB A:ASP10 4.5 22.7 1.0
O A:HOH246 4.5 27.8 1.0
CE1 A:HIS24 4.5 23.3 1.0
N A:PRO13 4.5 29.0 1.0
C A:PRO13 4.5 31.2 1.0
N A:TYR12 4.6 26.9 1.0
CB A:ARG228 4.6 31.1 1.0
ND2 A:ASN14 4.6 31.4 1.0
CB A:TYR12 4.6 28.2 1.0
O A:ASP208 4.7 25.5 1.0
CA A:ASN14 4.7 35.1 1.0
CB A:ASP19 4.7 36.2 1.0
OD1 A:ASP208 4.7 24.7 1.0
CD1 A:TYR12 4.8 31.0 1.0
NE2 A:HIS24 4.8 22.7 1.0
CA A:ARG228 4.8 30.9 1.0
O A:ARG228 4.9 29.6 1.0

Reference:

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
Page generated: Sat Dec 12 04:16:30 2020

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