Structure of IDP04461
Crystal structure of dihydroorotase pyrC from Yersinia pestis in complex with zinc and malate at 2.4 A resolution
Edit deposit information
- CSGID target
- IDP04461
- PDB Id
- 6CTY (NCBI MMDB)
- Authors
- 'J.Lipowska,I.G.Shabalin,J.Winsor,M.Woinska,D.R.Cooper,K.Kwon,L.Shuvalova,W.F.Anderson,W.Minor,Center For Structural Genomics Of Infectious Diseases (Csgid)'
- Responsible person
- Joanna Lipowska
- Responsible lab
- University of Virginia
- Deposition Date
- Mar 23, 2018
- Release Date
- Mar 15, 2017
Annotation
- Description
- Dihydroorotase catalyzes the formation of N-carbamoyl-L-aspartate from (S)-dihydroorotate in pyrimidine biosynthesis. This structure is a structure of dihydroorotase from the pathogen Yersinia pestis CO92, the causative agent of the systemic invasive infectious disease classically referred to as the plague and it has been responsible for human pandemics.The structure has an unknown ligand in the active site. Most likely it is L-aspartate or L-malic acid.
- Functional assignment
Ligands
| Ligand code | Name | Ligand type |
|---|---|---|
| KCX | modified residue | |
| CSX | modified residue | |
| UNL | crystallization | |
| ZN | zinc | biological |
Structure information
Unit cell parameters
- Space Group
- P 21 21 21
- Unit Cell
-
a=95.84Å, b=112.20Å, c=208.26Å
α=90.00, β=90.00, γ=90.00 - Solvent content
- Matthews coefficient
- Resolution range
- 50.01-2.41Å (2.47-2.41Å)
- Rall(%)
- 16.2
- Rwork(%)
- 16.0 (21.8)
- Rfree(%)
- 19.9 (26.4)
- Num. observed reflections
- 77855 (4215)
- Num. Rfree reflections
- 3892 (201)
- Completeness(%)
- 88.8 (65.8)
- Num Atoms
- 15894
- Num Waters
- 1083
- Num Hetatoms
- 1251
- Model mean isotropic B factor
- 44.550Å2
- RMSD bond length
- 0.010Å
- RMSD bond angle
- 1.375°
- Filename uploaded
- hkl_refine_122.pdb (uploaded on Feb 28, 2017 1:07 PM)
- Inserted
- Feb 28, 2017