Download MendeleyCrystal Structure of Glycerophosphoryl Diester Phosphodiesterase Domain of Uncharacterized Protein Rv2277c from Mycobacterium tuberculosis
Kim, Y., Li, H., Endres, M., Joachimiak, A.To be published.
5VUG
Crystal Structure of Glycerophosphoryl Diester Phosphodiesterase Domain of Uncharacterized Protein Rv2277c from Mycobacterium tuberculosis
- PDB DOI: https://doi.org/10.2210/pdb5VUG/pdb
- Classification: Structural genomics, Unknown function
- Organism(s): Mycobacterium tuberculosis H37Rv
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2017-05-19 Released: 2017-06-14
- Funding Organization(s): National Institutes of Health
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.50 Å
- R-Value Free: 0.196
- R-Value Work: 0.163
- R-Value Observed: 0.165
wwPDB Validation 3D Report Full Report
This is version 1.1 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Uncharacterized protein Rv2277c | 281 | Mycobacterium tuberculosis H37Rv | Mutation(s): 0 Gene Names: Rv2277c, MTCY339.33 |  | |
UniProt | |||||
Find proteins for P9WLF1 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)) Explore P9WLF1 Go to UniProtKB: P9WLF1 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P9WLF1 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GOL Query on GOL | C [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| CA Query on CA | B [auth A] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.50 Å
- R-Value Free: 0.196
- R-Value Work: 0.163
- R-Value Observed: 0.165
- Space Group: P 21 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 112.269 | α = 90 |
| b = 43.878 | β = 90 |
| c = 68.611 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| HKL-3000 | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2017-06-14 Deposition Author(s): Kim, Y., Li, H., Endres, M., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health | United States | -- |
Revision History (Full details and data files)
- Version 1.0: 2017-06-14
Type: Initial release - Version 1.1: 2017-09-20
Changes: Author supporting evidence
