Download MendeleyCrystal structure of NTF2-like protein of unknown function (YP_440611.1) from Burkholderia thailandensis E264 at 1.60 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
3EC9
CRYSTAL STRUCTURE OF A NTF2-like protein (BTH_I0051) FROM BURKHOLDERIA THAILANDENSIS E264 AT 1.60 A RESOLUTION
- PDB DOI: https://doi.org/10.2210/pdb3EC9/pdb
- Classification: UNKNOWN FUNCTION
- Organism(s): Burkholderia thailandensis E264
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2008-08-29 Released: 2008-09-09
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.60 Å
- R-Value Free: 0.198
- R-Value Work: 0.168
- R-Value Observed: 0.169
wwPDB Validation 3D Report Full Report
This is version 1.4 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 NTF2-like protein | 140 | Burkholderia thailandensis E264 | Mutation(s): 0 Gene Names: YP_440611.1, BTH_I0051 |  | |
UniProt | |||||
Find proteins for Q2T2I4 (Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264)) Explore Q2T2I4 Go to UniProtKB: Q2T2I4 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q2T2I4 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GOL Query on GOL | H [auth B] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| ACT Query on ACT | C [auth A], D [auth A], E [auth B], F [auth B], G [auth B] | ACETATE ION C2 H3 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-M |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.60 Å
- R-Value Free: 0.198
- R-Value Work: 0.168
- R-Value Observed: 0.169
- Space Group: P 21 21 21
- Diffraction Data: https://doi.org/10.18430/M33EC9
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 51.849 | α = 90 |
| b = 52.021 | β = 90 |
| c = 111.494 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PHENIX | refinement |
| SHELX | phasing |
| MolProbity | model building |
| SCALA | data scaling |
| PDB_EXTRACT | data extraction |
| MOSFLM | data reduction |
| SHELXD | phasing |
| autoSHARP | phasing |
Entry History
Deposition Data
- Released Date: 2008-09-09 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2008-09-09
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.2: 2017-10-25
Changes: Refinement description - Version 1.3: 2019-07-24
Changes: Data collection, Derived calculations, Refinement description - Version 1.4: 2023-02-01
Changes: Database references, Derived calculations
