Download MendeleyCrystal structure of hypothetical protein (YP_049261.1) from Erwinia carotovora subsp. atroseptica SCRI1043 at 2.40 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
2PG3
Crystal structure of a Queuosine biosynthesis protein queC (ECA1155) from Erwinia carotovora subsp. atroseptica SCRI1043 at 2.40 A resolution
- PDB DOI: https://doi.org/10.2210/pdb2PG3/pdb
- Classification: HYDROLASE
- Organism(s): Pectobacterium atrosepticum SCRI1043
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2007-04-06 Released: 2007-04-24
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.40 Å
- R-Value Free: 0.223
- R-Value Work: 0.186
- R-Value Observed: 0.188
wwPDB Validation 3D Report Full Report
This is version 1.6 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 |
| Queuosine biosynthesis protein queC | 232 | Pectobacterium atrosepticum SCRI1043 | Mutation(s): 3 Gene Names: YP_049261.1, queC, ECA1155 EC: 3.5 |  | |
UniProt | |||||
Find proteins for Q6D820 (Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)) Explore Q6D820 Go to UniProtKB: Q6D820 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q6D820 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| ZN Query on ZN | B [auth A] | ZINC ION Zn PTFCDOFLOPIGGS-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: 2.40 Å
- R-Value Free: 0.223
- R-Value Work: 0.186
- R-Value Observed: 0.188
- Space Group: P 41 21 2
- Diffraction Data: https://doi.org/10.18430/M32PG3
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 78.154 | α = 90 |
| b = 78.154 | β = 90 |
| c = 77.755 | γ = 90 |
| Software Name | Purpose |
|---|---|
| MolProbity | model building |
| SOLVE | phasing |
| REFMAC | refinement |
| SCALA | data scaling |
| PDB_EXTRACT | data extraction |
| MAR345 | data collection |
| MOSFLM | data reduction |
| CCP4 | data scaling |
Entry History
Deposition Data
- Released Date: 2007-04-24 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2007-04-24
Type: Initial release - Version 1.1: 2008-05-01
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Advisory, Derived calculations, Version format compliance - Version 1.3: 2014-12-24
Changes: Structure summary - Version 1.4: 2017-10-18
Changes: Refinement description - Version 1.5: 2017-10-25
Changes: Author supporting evidence - Version 1.6: 2023-01-25
Changes: Database references, Derived calculations
