Manganese in PDB 1ef2: Crystal Structure of Manganese-Substituted Klebsiella Aerogenes Urease

All present enzymatic activity of Crystal Structure of Manganese-Substituted Klebsiella Aerogenes Urease:
3.5.1.5;

The structure of Crystal Structure of Manganese-Substituted Klebsiella Aerogenes Urease, PDB code: 1ef2 was solved by K.Yamaguchi, N.J.Cosper, C.Stalhandske, R.A.Scott, M.A.Pearson, P.A.Karplus, R.P.Hausinger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.50
Space group	I 21 3
Cell size a, b, c (Å), α, β, γ (°)	170.800, 170.800, 170.800, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / n/a

The binding sites of Manganese atom in the Crystal Structure of Manganese-Substituted Klebsiella Aerogenes Urease (pdb code 1ef2). 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 Manganese-Substituted Klebsiella Aerogenes Urease, PDB code: 1ef2:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of Manganese-Substituted Klebsiella Aerogenes Urease


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 Manganese-Substituted Klebsiella Aerogenes Urease within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn4774 b:17.0 occ:0.95 ND1 A:HIS1246 2.2 15.0 1.0 O A:HOH500 2.2 20.0 1.0 OQ1 A:KCX1217 2.2 22.0 1.0 NE2 A:HIS1272 2.6 2.5 1.0 O A:HOH501 2.8 20.0 0.7 CE1 A:HIS1246 2.9 16.9 1.0 CX A:KCX1217 3.2 17.4 1.0 CG A:HIS1246 3.3 13.8 1.0 CD2 A:HIS1272 3.4 3.2 1.0 O A:GLY1277 3.4 8.2 1.0 OQ2 A:KCX1217 3.4 19.6 1.0 MN A:MN4775 3.4 17.0 1.0 NE2 A:HIS1219 3.6 10.9 1.0 CE1 A:HIS1272 3.6 2.0 1.0 O A:HOH502 3.8 20.0 0.7 CB A:HIS1246 3.8 13.6 1.0 CD2 A:HIS1219 4.0 8.7 1.0 NE2 A:HIS1246 4.1 17.2 1.0 CD2 A:HIS1246 4.3 15.5 1.0 NZ A:KCX1217 4.3 15.8 1.0 OD1 A:ASP1360 4.5 49.2 1.0 NE2 A:HIS1134 4.5 2.0 1.0 CG A:HIS1272 4.5 5.5 1.0 CE1 A:HIS1219 4.5 11.9 1.0 C A:GLY1277 4.5 6.6 1.0 CE1 A:HIS1134 4.6 6.3 1.0 ND1 A:HIS1272 4.6 3.9 1.0 CE A:KCX1217 4.9 10.5 1.0 CE1 A:HIS1320 4.9 43.4 1.0 O A:ALA1167 4.9 6.0 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of Manganese-Substituted Klebsiella Aerogenes Urease


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 Manganese-Substituted Klebsiella Aerogenes Urease within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn4775 b:17.0 occ:1.00 OQ2 A:KCX1217 2.1 19.6 1.0 O A:HOH500 2.2 20.0 1.0 NE2 A:HIS1136 2.3 2.0 1.0 OD2 A:ASP1360 2.4 55.4 1.0 O A:HOH502 2.4 20.0 0.7 NE2 A:HIS1134 2.6 2.0 1.0 CX A:KCX1217 3.0 17.4 1.0 CG A:ASP1360 3.1 27.1 1.0 CD2 A:HIS1136 3.3 4.5 1.0 OQ1 A:KCX1217 3.3 22.0 1.0 OD1 A:ASP1360 3.3 49.2 1.0 CE1 A:HIS1136 3.3 3.5 1.0 O A:HOH501 3.4 20.0 0.7 MN A:MN4774 3.4 17.0 0.9 CD2 A:HIS1134 3.5 3.6 1.0 CE1 A:HIS1134 3.6 6.3 1.0 NZ A:KCX1217 4.2 15.8 1.0 O A:ALA1167 4.2 6.0 1.0 CG2 A:THR1169 4.2 4.6 1.0 O A:ALA1363 4.3 7.4 1.0 CB A:ASP1360 4.4 4.6 1.0 ND1 A:HIS1136 4.4 3.1 1.0 CG A:HIS1136 4.4 3.4 1.0 CB A:ALA1363 4.5 6.8 1.0 CG A:HIS1134 4.7 6.3 1.0 ND1 A:HIS1134 4.7 7.3 1.0 CA A:ASP1360 4.8 5.4 1.0 OG1 A:THR1169 4.9 9.7 1.0 NE2 A:HIS1219 4.9 10.9 1.0 N A:THR1169 5.0 8.5 1.0

K.Yamaguchi, N.J.Cosper, C.Stalhandske, R.A.Scott, M.A.Pearson, P.A.Karplus, R.P.Hausinger. Characterization of Metal-Substituted Klebsiella Aerogenes Urease. J.Biol.Inorg.Chem. V. 4 468 1999.
ISSN: ISSN 0949-8257
PubMed: 10555581
DOI: 10.1007/S007750050333