Structure of IDP91189
Crystal structure of aminoglycoside phosphotransferase APH(2")-Id/APH(2")-IVa in complex with HEPES
Edit deposit information
- CSGID target
- IDP91189
- PDB Id
- 4DE4 (NCBI MMDB)
- Authors
- P.J.Stogios,G.Minasov,K.Tan,B.Nocek,E.Evdokimova,O.Egorova,R.Di Leo,H.Li,A.Savchenko,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid)
- Responsible person
- Peter Stogios
- Responsible lab
- University of Calgary
- Deposition Date
- Jan 19, 2012
- Release Date
- Feb 08, 2012
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 gentamicin-bound structure of APH(2'')-Id/APH(2'')-IVa, an enzyme that acts on gentamicin and kanamycin.
- Functional assignment
- kinase
Ligands
| Ligand code | Name | Ligand type |
|---|---|---|
| EPE | crystallization | |
| 175 | 3,5-dihydro-5-methylidene-4h-imidazol-4-on |
Structure information
Unit cell parameters
- Space Group
- P 1 21 1
- Unit Cell
-
a=42.54Å, b=101.21Å, c=71.17Å
α=90.00, β=97.51, γ=90.00 - Solvent content
- Matthews coefficient
- Resolution range
- 28.99-2.00Å (2.07-2.00Å)
- Rall(%)
- 22.4
- Rwork(%)
- 22.2 (31.8)
- Rfree(%)
- 27.2 (36.0)
- Num. observed reflections
- 40668 (3668)
- Num. Rfree reflections
- 2102 (190)
- Completeness(%)
- 95.9 (92.0)
- Num Atoms
- 4799
- Num Waters
- 270
- Num Hetatoms
- 439
- Model mean isotropic B factor
- 48.430Å2
- RMSD bond length
- 0.002Å
- RMSD bond angle
- 0.599°
- RMSD dihedral angle
- 11.448°
- Filename uploaded
- 4DE4.pdb (uploaded on Feb 14, 2012 9:26 AM)
- Inserted
- Mar 23, 2011