Manganese in PDB 2r34: Crystal Structure of Mn Human Arg-Insulin

The structure of Crystal Structure of Mn Human Arg-Insulin, PDB code: 2r34 was solved by R.Sreekanth, V.Pattabhi, S.S.Rajan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.36 / 2.25
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	80.687, 80.687, 37.517, 90.00, 90.00, 120.00
R / Rfree (%)	18.6 / 26.4

The structure of Crystal Structure of Mn Human Arg-Insulin also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Manganese atom in the Crystal Structure of Mn Human Arg-Insulin (pdb code 2r34). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Mn Human Arg-Insulin, PDB code: 2r34:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Mn Human Arg-Insulin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Mn Human Arg-Insulin within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn32 b:20.0 occ:0.33 NE2 B:HIS10 2.2 28.0 1.0 CL B:CL31 2.4 29.3 0.3 CD2 B:HIS10 3.0 23.7 1.0 CE1 B:HIS10 3.3 27.8 1.0 CG B:HIS10 4.2 17.9 1.0 ND1 B:HIS10 4.3 18.2 1.0 O B:LEU6 4.5 27.2 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Mn Human Arg-Insulin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Mn Human Arg-Insulin within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn32 b:23.4 occ:0.33 NE2 D:HIS10 2.2 27.5 1.0 CL D:CL31 2.5 64.3 0.3 CD2 D:HIS10 3.0 22.5 1.0 CE1 D:HIS10 3.3 20.2 1.0 CG D:HIS10 4.2 19.8 1.0 ND1 D:HIS10 4.3 14.5 1.0 O D:HOH52 4.7 47.0 1.0

R.Sreekanth, V.Pattabhi, S.S.Rajan. Metal Induced Structural Changes Observed in Hexameric Insulin Int.J.Biol.Macromol. V. 44 29 2009.
ISSN: ISSN 0141-8130
PubMed: 18977386
DOI: 10.1016/J.IJBIOMAC.2008.09.019