Manganese in PDB 3qh8: Crystal Structure of A Beta-Lactamase-Like Protein Bound to Amp From Brucella Melitensis, Long Wavelength Synchrotron Data

The structure of Crystal Structure of A Beta-Lactamase-Like Protein Bound to Amp From Brucella Melitensis, Long Wavelength Synchrotron Data, PDB code: 3qh8 was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	18.88 / 1.60
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	73.210, 75.530, 98.940, 90.00, 90.00, 90.00
R / Rfree (%)	14.3 / 16.6

The structure of Crystal Structure of A Beta-Lactamase-Like Protein Bound to Amp From Brucella Melitensis, Long Wavelength Synchrotron Data also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Manganese atom in the Crystal Structure of A Beta-Lactamase-Like Protein Bound to Amp From Brucella Melitensis, Long Wavelength Synchrotron Data (pdb code 3qh8). 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 A Beta-Lactamase-Like Protein Bound to Amp From Brucella Melitensis, Long Wavelength Synchrotron Data, PDB code: 3qh8:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Crystal Structure of A Beta-Lactamase-Like Protein Bound to Amp From Brucella Melitensis, Long Wavelength Synchrotron Data


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 A Beta-Lactamase-Like Protein Bound to Amp From Brucella Melitensis, Long Wavelength Synchrotron Data within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn300 b:10.8 occ:1.00 O A:HOH340 2.1 12.0 1.0 NE2 A:HIS241 2.2 7.2 1.0 OD2 A:ASP188 2.3 9.0 1.0 OD2 A:ASP90 2.3 7.5 1.0 NE2 A:HIS91 2.3 7.9 1.0 O3P A:AMP303 2.4 20.9 1.0 CG A:ASP188 3.0 8.8 1.0 OD1 A:ASP188 3.1 11.4 1.0 CD2 A:HIS91 3.1 8.0 1.0 CE1 A:HIS241 3.2 8.6 1.0 CD2 A:HIS241 3.2 9.4 1.0 CG A:ASP90 3.2 9.1 1.0 CE1 A:HIS91 3.3 7.9 1.0 OD1 A:ASP90 3.4 10.4 1.0 MN A:MN301 3.4 9.2 1.0 P A:AMP303 3.6 20.7 1.0 O1P A:AMP303 4.0 13.6 1.0 O A:HOH376 4.2 9.0 1.0 O5' A:AMP303 4.2 18.3 1.0 CE1 A:HIS86 4.3 7.0 1.0 NE2 A:HIS86 4.3 6.7 1.0 ND1 A:HIS241 4.3 11.0 1.0 CG A:HIS241 4.3 9.0 1.0 CG A:HIS91 4.3 7.5 1.0 ND1 A:HIS91 4.4 9.7 1.0 CE1 A:HIS219 4.5 9.7 1.0 CB A:ASP188 4.5 8.7 1.0 CB A:ASP90 4.6 8.9 1.0 O2P A:AMP303 4.8 20.1 1.0 CB A:SER18 5.0 9.0 1.0

Manganese binding site 2 out of 2 in the Crystal Structure of A Beta-Lactamase-Like Protein Bound to Amp From Brucella Melitensis, Long Wavelength Synchrotron Data


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 A Beta-Lactamase-Like Protein Bound to Amp From Brucella Melitensis, Long Wavelength Synchrotron Data within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn301 b:9.2 occ:1.00 O A:HOH340 2.1 12.0 1.0 NE2 A:HIS86 2.2 6.7 1.0 O1P A:AMP303 2.2 13.6 1.0 ND1 A:HIS88 2.2 9.5 1.0 NE2 A:HIS170 2.2 10.0 1.0 OD2 A:ASP188 2.4 9.0 1.0 CE1 A:HIS170 3.1 9.8 1.0 CD2 A:HIS86 3.2 6.9 1.0 CE1 A:HIS88 3.2 10.9 1.0 CE1 A:HIS86 3.2 7.0 1.0 CG A:HIS88 3.3 8.4 1.0 CD2 A:HIS170 3.3 10.0 1.0 P A:AMP303 3.3 20.7 1.0 MN A:MN300 3.4 10.8 1.0 CG A:ASP188 3.4 8.8 1.0 O3P A:AMP303 3.6 20.9 1.0 CB A:HIS88 3.6 7.3 1.0 CB A:ASP188 3.9 8.7 1.0 O5' A:AMP303 4.0 18.3 1.0 C5' A:AMP303 4.2 16.2 1.0 ND1 A:HIS170 4.3 8.7 1.0 NE2 A:HIS88 4.3 11.5 1.0 NE2 A:HIS91 4.3 7.9 1.0 CG A:HIS86 4.3 7.1 1.0 ND1 A:HIS86 4.3 7.5 1.0 CD2 A:HIS88 4.4 8.8 1.0 CG A:HIS170 4.4 8.4 1.0 OD1 A:ASP188 4.4 11.4 1.0 CD2 A:HIS91 4.5 8.0 1.0 OD1 A:ASP90 4.6 10.4 1.0 O2P A:AMP303 4.6 20.1 1.0 CE1 A:HIS219 4.8 9.7 1.0

J.Abendroth, B.Sankaran, T.E.Edwards, A.S.Gardberg, S.Dieterich, J.Bhandari, A.J.Napuli, W.C.Van Voorhis, B.L.Staker, P.J.Myler, L.J.Stewart. Crystal Structure of A Beta-Lactamase-Like Protein Bound to Amp From Brucella Melitensis, Long Wavelength Synchrotron Data Acta Crystallogr.,Sect.F V. 67 1106 2011.
ISSN: ESSN 1744-3091
PubMed: 21904058
DOI: 10.1107/S1744309111010220