Manganese in PDB 1dq5: Manganese;Manganese Concanavalin A at pH 5.0

The structure of Manganese;Manganese Concanavalin A at pH 5.0, PDB code: 1dq5 was solved by J.Bouckaert, Y.Dewallef, F.Poortmans, L.Wyns, R.Loris, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.00
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	63.230, 87.440, 89.270, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 21

The binding sites of Manganese atom in the Manganese;Manganese Concanavalin A at pH 5.0 (pdb code 1dq5). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Manganese;Manganese Concanavalin A at pH 5.0, PDB code: 1dq5:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Manganese;Manganese Concanavalin A at pH 5.0


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Manganese;Manganese Concanavalin A at pH 5.0 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn301 b:28.0 occ:1.00 O A:HOH306 2.0 18.3 1.0 OD2 A:ASP10 2.2 22.8 1.0 NE2 A:HIS24 2.3 13.6 1.0 O A:HOH319 2.3 26.3 1.0 OE2 A:GLU8 2.3 16.4 1.0 OD1 A:ASP19 2.5 30.9 1.0 CD2 A:HIS24 3.2 14.7 1.0 CD A:GLU8 3.2 15.6 1.0 CG A:ASP10 3.2 21.1 1.0 CE1 A:HIS24 3.3 15.1 1.0 CG A:ASP19 3.4 30.8 1.0 OE1 A:GLU8 3.5 15.3 1.0 CB A:ASP10 3.5 20.7 1.0 OD2 A:ASP19 3.8 30.8 1.0 O A:HOH376 4.0 38.3 1.0 OG A:SER34 4.2 23.2 1.0 O A:HOH361 4.2 34.7 1.0 MN A:MN302 4.3 30.2 1.0 OD1 A:ASP10 4.3 21.3 1.0 CG A:HIS24 4.4 15.5 1.0 ND1 A:HIS24 4.4 15.2 1.0 CB A:ASP19 4.5 31.1 1.0 O A:VAL32 4.5 23.6 1.0 CG A:GLU8 4.6 16.1 1.0 CA A:ASP19 4.6 31.9 1.0

Manganese binding site 2 out of 2 in the Manganese;Manganese Concanavalin A at pH 5.0


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Manganese;Manganese Concanavalin A at pH 5.0 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn302 b:30.2 occ:1.00 O A:TYR12 2.2 28.1 1.0 OD2 A:ASP19 2.2 30.8 1.0 OD1 A:ASP10 2.3 21.3 1.0 O A:HOH364 2.5 35.1 1.0 O A:HOH361 2.5 34.7 1.0 OD2 A:ASP10 2.5 22.8 1.0 OD1 A:ASN14 2.6 27.7 1.0 CG A:ASP10 2.7 21.1 1.0 CG A:ASP19 3.3 30.8 1.0 C A:TYR12 3.4 28.3 1.0 CG A:ASN14 3.8 28.1 1.0 OD1 A:ASP19 3.8 30.9 1.0 N A:ASN14 4.0 30.0 1.0 N A:TYR12 4.2 26.0 1.0 CB A:ASP10 4.2 20.7 1.0 CA A:TYR12 4.2 27.5 1.0 MN A:MN301 4.3 28.0 1.0 CB A:ASN14 4.4 27.8 1.0 N A:PRO13 4.4 29.1 1.0 CE1 A:HIS24 4.5 15.1 1.0 CB A:TYR12 4.5 28.4 1.0 CA A:PRO13 4.6 29.7 1.0 O A:ASP208 4.6 20.2 1.0 OD1 A:ASP208 4.6 22.1 1.0 O A:HOH306 4.6 18.3 1.0 CB A:ASP19 4.6 31.1 1.0 C A:PRO13 4.7 29.8 1.0 NE2 A:HIS24 4.7 13.6 1.0 CA A:ASN14 4.8 30.1 1.0 CA A:ASP10 4.8 20.3 1.0 O A:ARG228 4.8 20.0 1.0 ND2 A:ASN14 4.9 27.4 1.0 C A:ASP10 5.0 21.7 1.0 CB A:ARG228 5.0 22.1 1.0

J.Bouckaert, Y.Dewallef, F.Poortmans, L.Wyns, R.Loris. The Structural Features of Concanavalin A Governing Non-Proline Peptide Isomerization J.Biol.Chem. V. 275 19778 2000.
ISSN: ISSN 0021-9258
PubMed: 10748006
DOI: 10.1074/JBC.M001251200