Download MendeleyX-ray crystal structure of conserved hypothetical SPy1581 protein from Streptococcus pyogenes.
Osipiuk, J., Lezondra, L., Moy, S., Collart, F., Joachimiak, A.To be published.
1YHF | pdb_00001yhf
Crystal Structure of Conserved SPY1581 Protein of Unknown Function from Streptococcus pyogenes
- PDB DOI: https://doi.org/10.2210/pdb1YHF/pdb
- Classification: STRUCTURAL GENOMICS, UNKNOWN FUNCTION
- Organism(s): Streptococcus pyogenes M1 GAS
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2005-01-07 Released: 2005-02-22
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.00 Å
- R-Value Free: 0.248 (Depositor), 0.209 (DCC)
- R-Value Work: 0.190 (Depositor), 0.190 (DCC)
- R-Value Observed: 0.192 (Depositor)
wwPDB Validation 3D Report Full Report
This is version 1.3 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 |
| hypothetical protein SPy1581 | 115 | Streptococcus pyogenes M1 GAS | Mutation(s): 6 Gene Names: SPy1581 |  | |
UniProt | |||||
Find proteins for Q99YR1 (Streptococcus pyogenes serotype M1) Explore Q99YR1 Go to UniProtKB: Q99YR1 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q99YR1 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| 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: 2.00 Å
- R-Value Free: 0.248 (Depositor), 0.209 (DCC)
- R-Value Work: 0.190 (Depositor), 0.190 (DCC)
- R-Value Observed: 0.192 (Depositor)
Space Group: P 41 2 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 39.897 | α = 90 |
| b = 39.897 | β = 90 |
| c = 144.758 | γ = 90 |
| Software Name | Purpose |
|---|---|
| SCALEPACK | data scaling |
| MLPHARE | phasing |
| DM | phasing |
| REFMAC | refinement |
| HKL-2000 | data reduction |
Entry History
Deposition Data
- Released Date: 2005-02-22 Deposition Author(s): Osipiuk, J., Lezondra, L., Moy, S., Collart, F., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2005-02-22
Type: Initial release - Version 1.1: 2008-04-30
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Advisory, Derived calculations, Source and taxonomy, Version format compliance - Version 1.3: 2024-11-20
Changes: Data collection, Database references, Derived calculations, Structure summary
