Structure of IDP91779
Crystal structure of lincosamide antibiotic adenylyltransferase LnuA, apo
Edit deposit information
- CSGID target
- IDP91779
- PDB Id
- 4FO1 (NCBI MMDB)
- Authors
- 'P.J.Stogios,Z.Wawrzak,G.Minasov,E.Evdokimova,O.Egorova,M.Kudritska,V.Yim,P.Courvalin,A.Savchenko,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid)'
- Responsible person
- Peter Stogios
- Responsible lab
- University of Calgary
- Deposition Date
- Jun 20, 2012
- Release Date
- Apr 04, 2012
Annotation
- Description
- One mechanism of resistance to the antibiotic lincomycin, a compound that is used to treat numerous infections, is conferred by adenylation by enzymes of the lin family. In this entry, we demonstrate the structure of LinA in the apo and lincomycin-bound forms. The enzyme adopts a structure similar to LinB (PDB 3JZO), but also shows some novel features including an insertion of approximately six residues in the active site, and a novel dimerization mechanism.
- Functional assignment
- nucleotidyltransferase
Ligands
| Ligand code | Name | Ligand type |
|---|---|---|
| MSE | modified residue | |
| 175 | 3,5-dihydro-5-methylidene-4h-imidazol-4-on |
Structure information
Unit cell parameters
- Space Group
- P 1 21 1
- Unit Cell
-
a=57.39Å, b=61.91Å, c=61.34Å
α=90.00, β=103.24, γ=90.00 - Solvent content
- Matthews coefficient
- Resolution range
- 29.86-2.15Å (2.25-2.15Å)
- Rall(%)
- 21.8
- Rwork(%)
- 21.5 (25.0)
- Rfree(%)
- 26.2 (35.5)
- Num. observed reflections
- 23438 (2505)
- Num. Rfree reflections
- 1164 (130)
- Completeness(%)
- 97.3 (92.0)
- Num Atoms
- 2638
- Num Waters
- 223
- Num Hetatoms
- 333
- Model mean isotropic B factor
- 53.610Å2
- RMSD bond length
- 0.003Å
- RMSD bond angle
- 0.763°
- RMSD dihedral angle
- 17.343°
- Filename uploaded
- 4FO1.pdb (uploaded on Apr 30, 2014 9:02 AM)
- Inserted
- Mar 26, 2012