Manganese in PDB 1ir6: Crystal Structure of Exonuclease Recj Bound to Manganese

The structure of Crystal Structure of Exonuclease Recj Bound to Manganese, PDB code: 1ir6 was solved by A.Yamagata, Y.Kakuta, R.Masui, K.Fukuyama, Riken Structuralgenomics/Proteomics Initiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.83 / 2.90
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	141.600, 141.600, 141.600, 90.00, 90.00, 90.00
R / Rfree (%)	22.8 / 25.9

The binding sites of Manganese atom in the Crystal Structure of Exonuclease Recj Bound to Manganese (pdb code 1ir6). 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 Crystal Structure of Exonuclease Recj Bound to Manganese, PDB code: 1ir6:

Manganese binding site 1 out of 1 in the Crystal Structure of Exonuclease Recj Bound to Manganese


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 Exonuclease Recj Bound to Manganese within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1434 b:61.6 occ:1.00 NE2 A:HIS160 2.2 72.1 1.0 OD2 A:ASP84 2.4 52.3 1.0 OD2 A:ASP221 2.5 74.8 1.0 OD1 A:ASP136 2.6 71.2 1.0 OD2 A:ASP136 2.6 69.8 1.0 CG A:ASP136 3.0 68.9 1.0 CE1 A:HIS160 3.2 70.6 1.0 CG A:ASP221 3.2 74.4 1.0 CD2 A:HIS160 3.2 71.5 1.0 NE2 A:HIS161 3.2 79.7 1.0 CG A:ASP84 3.4 53.4 1.0 OD1 A:ASP221 3.4 74.8 1.0 CB A:ASP84 3.7 52.3 1.0 CD2 A:HIS161 3.9 79.2 1.0 N A:GLY187 4.2 63.4 1.0 ND1 A:HIS160 4.3 70.5 1.0 CE1 A:HIS161 4.3 79.3 1.0 CG A:HIS160 4.3 70.8 1.0 CB A:ASP221 4.5 73.6 1.0 CB A:ASP136 4.5 66.7 1.0 OD1 A:ASP84 4.5 55.3 1.0 OD1 A:ASP82 4.5 62.0 1.0 CA A:GLY187 4.6 62.8 1.0 OD2 A:ASP82 4.7 67.5 1.0

A.Yamagata, Y.Kakuta, R.Masui, K.Fukuyama. The Crystal Structure of Exonuclease Recj Bound to MN2+ Ion Suggests How Its Characteristic Motifs Are Involved in Exonuclease Activity. Proc.Natl.Acad.Sci.Usa V. 99 5908 2002.
ISSN: ISSN 0027-8424
PubMed: 11972066
DOI: 10.1073/PNAS.092547099