Structure of IDP91187
Crystal structure of aminoglycoside phosphotransferase APH(2")-Ib/APH(2'')-IIa, apo form
Edit deposit information
- CSGID target
- IDP91187
- PDB Id
- 3UZR (NCBI MMDB)
- Authors
- P.J.Stogios,G.Minasov,A.U.Singer,K.Tan,B.Nocek,E.Evdokimova,E.Egorova,R.Di Leo,A.Savchenko,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid)
- Responsible person
- Peter Stogios
- Responsible lab
- University of Calgary
- Deposition Date
- Dec 07, 2011
- Release Date
- Dec 21, 2011
Annotation
- Description
- Aminoglycoside phosphotransferase (APH) enzymes act in a substrate- and position-specific manner and confer resistance to the activity of various aminoglycoside antibiotics. APH enzymes show a eukaryotic protein kinase-like fold with an insertion that takes part in substrate recognition. This is the apo structure of APH(2'')-Ib, an enzyme that acts on gentamicin, kanamycin, neomycin and other aminoglycosides.
- Functional assignment
- kinase
Ligands
| Ligand code | Name | Ligand type |
|---|---|---|
| EDO | ethylene diol | crystallization |
| MG | magnesium | crystallization |
| MSE | modified residue | |
| PEG | crystallization | |
| 175 | 3,5-dihydro-5-methylidene-4h-imidazol-4-on |
Structure information
Unit cell parameters
- Space Group
- P 2 21 21
- Unit Cell
-
a=60.72Å, b=62.22Å, c=89.73Å
α=90.00, β=90.00, γ=90.00 - Solvent content
- Matthews coefficient
- Resolution range
- 19.93-1.95Å (2.00-1.95Å)
- Rall(%)
- 19.6
- Rwork(%)
- 19.4 (28.1)
- Rfree(%)
- 24.5 (32.2)
- Num. observed reflections
- 23269 (1268)
- Num. Rfree reflections
- 1186 (60)
- Completeness(%)
- 91.6 (70.1)
- Num Atoms
- 2509
- Num Waters
- 261
- Num Hetatoms
- 360
- Model mean isotropic B factor
- 29.450Å2
- RMSD bond length
- 0.011Å
- RMSD bond angle
- 1.251°
- Filename uploaded
- 3UZR.pdb (uploaded on Feb 14, 2012 8:55 AM)
- Inserted
- Mar 23, 2011