Manganese in PDB 1jui: Concanavalin A-Carbohydrate Mimicking 10-Mer Peptide Complex

The structure of Concanavalin A-Carbohydrate Mimicking 10-Mer Peptide Complex, PDB code: 1jui was solved by D.Jain, K.J.Kaur, D.M.Salunke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.75
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	102.970, 118.330, 253.600, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 22.2

The structure of Concanavalin A-Carbohydrate Mimicking 10-Mer Peptide Complex also contains other interesting chemical elements:

Calcium

(Ca)

4 atoms

The binding sites of Manganese atom in the Concanavalin A-Carbohydrate Mimicking 10-Mer Peptide Complex (pdb code 1jui). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Concanavalin A-Carbohydrate Mimicking 10-Mer Peptide Complex, PDB code: 1jui:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Concanavalin A-Carbohydrate Mimicking 10-Mer Peptide Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Concanavalin A-Carbohydrate Mimicking 10-Mer Peptide Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:33.1 occ:1.00 O A:HOH440 2.2 37.8 1.0 OD2 A:ASP10 2.3 24.8 1.0 OE2 A:GLU8 2.3 26.4 1.0 NE2 A:HIS24 2.4 33.5 1.0 OD1 A:ASP19 2.5 44.2 1.0 CG A:ASP19 3.1 44.2 1.0 CE1 A:HIS24 3.2 33.5 1.0 CG A:ASP10 3.3 24.8 1.0 CD2 A:HIS24 3.4 33.5 1.0 OD2 A:ASP19 3.4 44.2 1.0 CD A:GLU8 3.4 26.4 1.0 CB A:ASP10 3.6 24.8 1.0 OE1 A:GLU8 3.8 26.4 1.0 O A:HOH425 3.9 42.1 1.0 OG A:SER34 4.0 27.4 1.0 O A:HOH431 4.1 51.0 1.0 ND1 A:HIS24 4.3 33.5 1.0 CB A:ASP19 4.3 44.2 1.0 OD1 A:ASP10 4.4 24.8 1.0 CG A:HIS24 4.5 33.5 1.0 CA A:CA402 4.5 33.1 1.0 CA A:ASP19 4.6 34.0 1.0 CG A:GLU8 4.7 26.4 1.0 O A:VAL32 4.7 23.2 1.0

Manganese binding site 2 out of 4 in the Concanavalin A-Carbohydrate Mimicking 10-Mer Peptide Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Concanavalin A-Carbohydrate Mimicking 10-Mer Peptide Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn403 b:33.1 occ:1.00 OE2 B:GLU8 2.3 39.9 1.0 NE2 B:HIS24 2.4 40.4 1.0 OD2 B:ASP10 2.4 34.1 1.0 OD1 B:ASP19 2.5 43.3 1.0 O B:HOH412 2.8 55.2 1.0 CD B:GLU8 3.2 39.9 1.0 CE1 B:HIS24 3.3 40.4 1.0 CG B:ASP19 3.3 43.3 1.0 CD2 B:HIS24 3.4 40.4 1.0 CG B:ASP10 3.4 34.1 1.0 OE1 B:GLU8 3.5 39.9 1.0 OD2 B:ASP19 3.6 43.3 1.0 CB B:ASP10 3.7 34.1 1.0 OG B:SER34 3.9 38.2 1.0 ND1 B:HIS24 4.4 40.4 1.0 CG B:HIS24 4.5 40.4 1.0 CA B:CA404 4.5 33.1 1.0 O B:VAL32 4.5 30.7 1.0 CB B:ASP19 4.5 43.3 1.0 OD1 B:ASP10 4.5 34.1 1.0 CG B:GLU8 4.6 39.9 1.0 CA B:ASP19 4.7 45.0 1.0

Manganese binding site 3 out of 4 in the Concanavalin A-Carbohydrate Mimicking 10-Mer Peptide Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Concanavalin A-Carbohydrate Mimicking 10-Mer Peptide Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Mn405 b:33.1 occ:1.00 OD2 C:ASP10 2.3 30.9 1.0 OE2 C:GLU8 2.3 34.5 1.0 NE2 C:HIS24 2.4 26.3 1.0 O C:HOH477 2.4 43.9 1.0 O C:HOH441 2.5 32.0 1.0 OD1 C:ASP19 2.5 48.2 1.0 CE1 C:HIS24 3.1 26.3 1.0 CG C:ASP19 3.1 48.2 1.0 CG C:ASP10 3.2 30.9 1.0 OD2 C:ASP19 3.4 48.2 1.0 CD C:GLU8 3.4 34.5 1.0 CD2 C:HIS24 3.4 26.3 1.0 CB C:ASP10 3.5 30.9 1.0 OE1 C:GLU8 3.8 34.5 1.0 OG C:SER34 4.1 39.0 1.0 ND1 C:HIS24 4.3 26.3 1.0 CB C:ASP19 4.3 48.2 1.0 OD1 C:ASP10 4.4 30.9 1.0 CA C:CA406 4.4 33.1 1.0 CG C:HIS24 4.5 26.3 1.0 CA C:ASP19 4.6 61.5 1.0 CG C:GLU8 4.7 34.5 1.0 O C:VAL32 4.7 33.4 1.0

Manganese binding site 4 out of 4 in the Concanavalin A-Carbohydrate Mimicking 10-Mer Peptide Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Concanavalin A-Carbohydrate Mimicking 10-Mer Peptide Complex within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn407 b:33.1 occ:1.00 OE2 D:GLU8 2.3 31.3 1.0 NE2 D:HIS24 2.3 30.2 1.0 OD2 D:ASP10 2.4 16.3 1.0 O D:HOH412 2.5 30.1 1.0 OD1 D:ASP19 2.6 31.6 1.0 CE1 D:HIS24 3.2 30.2 1.0 CD D:GLU8 3.2 31.3 1.0 CG D:ASP19 3.3 31.6 1.0 CD2 D:HIS24 3.3 30.2 1.0 CG D:ASP10 3.4 16.3 1.0 OE1 D:GLU8 3.5 31.3 1.0 OD2 D:ASP19 3.6 31.6 1.0 CB D:ASP10 3.7 16.3 1.0 OG D:SER34 3.9 33.5 1.0 O D:HOH422 4.0 49.3 1.0 O D:HOH461 4.3 46.9 1.0 ND1 D:HIS24 4.3 30.2 1.0 CG D:HIS24 4.4 30.2 1.0 CB D:ASP19 4.5 31.6 1.0 OD1 D:ASP10 4.5 16.3 1.0 CA D:CA408 4.5 33.1 1.0 O D:VAL32 4.6 24.6 1.0 CG D:GLU8 4.6 31.3 1.0 CA D:ASP19 4.7 40.2 1.0

D.Jain, K.J.Kaur, D.M.Salunke. Plasticity in Protein-Peptide Recognition: Crystal Structures of Two Different Peptides Bound to Concanavalin A. Biophys.J. V. 80 2912 2001.
ISSN: ISSN 0006-3495
PubMed: 11371463