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Structure paper

TitleThe Zn2 position in metallo-beta-lactamases is critical for activity: a study on chimeric metal sites on a conserved protein scaffold.
Journal, issue, pagesJ. Mol. Biol., Vol. 373, Page 1141-1156, Year 2007
Publish dateNov 17, 2006 (structure data deposition date)
AuthorsGonzalez, J.M. / Medrano Martin, F.J. / Costello, A.L. / Tierney, D.L. / Vila, A.J.
External linksJ. Mol. Biol. / PubMed:17915249
MethodsX-ray diffraction
Resolution1.8 - 2.29 Å
Structure data

PDB-2nxa:
Structure of Zn-dependent Metallo-Beta-Lactamase from Bacillus Cereus R121H, C221D Double Mutant
Method: X-RAY DIFFRACTION / Resolution: 2.29 Å

PDB-2nyp:
Structure of beta-lactamase II from Bacillus cereus. R121H, C221D doble mutant with two zinc ions.
Method: X-RAY DIFFRACTION / Resolution: 1.84 Å

PDB-2nze:
Structure of beta-lactamase II from Bacillus cereus. R121H, C221S double mutant. Space group P3121.
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2nzf:
Structure of beta-lactamase II from Bacillus cereus. R121H, C221S double mutant. Space group C2.
Method: X-RAY DIFFRACTION / Resolution: 2.28 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-ACY:
ACETIC ACID

ChemComp-GOL:
GLYCEROL

Source
  • bacillus cereus (bacteria)
KeywordsHYDROLASE / Bacillus cereus / R121H-C221D double mutant / Beta-lactamase II

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