Manganese in PDB 3cna: Structure of Concanavalin A at 2.4 Angstroms Resolution

The structure of Structure of Concanavalin A at 2.4 Angstroms Resolution, PDB code: 3cna was solved by K.D.Hardman, C.F.Ainsworth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 2.40
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	63.150, 86.910, 89.250, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of Structure of Concanavalin A at 2.4 Angstroms Resolution also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Manganese atom in the Structure of Concanavalin A at 2.4 Angstroms Resolution (pdb code 3cna). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Structure of Concanavalin A at 2.4 Angstroms Resolution, PDB code: 3cna:

Manganese binding site 1 out of 1 in the Structure of Concanavalin A at 2.4 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Concanavalin A at 2.4 Angstroms Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn238 b:0.0 occ:1.00 NE2 A:HIS24 2.1 0.0 1.0 OD1 A:ASP19 2.3 0.0 1.0 OD1 A:ASP10 2.7 0.0 1.0 OE2 A:GLU8 2.7 0.0 1.0 CE1 A:HIS24 2.7 0.0 1.0 O A:HOH240 2.8 0.0 1.0 O A:HOH241 2.8 0.0 1.0 CG A:ASP10 3.1 0.0 1.0 CD A:GLU8 3.1 0.0 1.0 CD2 A:HIS24 3.2 0.0 1.0 CB A:ASP10 3.3 0.0 1.0 CG A:ASP19 3.3 0.0 1.0 OE1 A:GLU8 3.3 0.0 1.0 OD2 A:ASP19 3.7 0.0 1.0 OD2 A:ASP10 3.9 0.0 1.0 ND1 A:HIS24 3.9 0.0 1.0 OG A:SER34 4.0 0.0 1.0 CG A:HIS24 4.2 0.0 1.0 O A:HOH243 4.2 0.0 1.0 CG A:GLU8 4.3 0.0 1.0 CD A:PRO20 4.3 0.0 1.0 CA A:CA239 4.5 0.0 1.0 CB A:ASP19 4.7 0.0 1.0 CA A:ASP10 4.8 0.0 1.0 O A:VAL32 4.9 0.0 1.0 CA A:ASP19 5.0 0.0 1.0

K.D.Hardman, C.F.Ainsworth. Structure of Concanavalin A at 2.4-A Resolution. Biochemistry V. 11 4910 1972.
ISSN: ISSN 0006-2960
PubMed: 4638345
DOI: 10.1021/BI00776A006