Download MendeleyCrystal structure of uncharacterized protein BH2621 (NP_243487.1) from Bacillus halodurans at 1.55 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
2QML
Crystal structure of an uncharacterized protein (bh2621) from bacillus halodurans at 1.55 A resolution
- PDB DOI: https://doi.org/10.2210/pdb2QML/pdb
- Classification: UNKNOWN FUNCTION
- Organism(s): Halalkalibacterium halodurans
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2007-07-16 Released: 2007-09-04
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.55 Å
- R-Value Free: 0.212
- R-Value Work: 0.179
- R-Value Observed: 0.181
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 |
| BH2621 protein | 198 | Halalkalibacterium halodurans | Mutation(s): 10 Gene Names: NP_243487.1, BH2621 |  | |
UniProt | |||||
Find proteins for Q9K9M4 (Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)) Explore Q9K9M4 Go to UniProtKB: Q9K9M4 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9K9M4 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| GOL Query on GOL | E [auth A], F [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| CL Query on CL | B [auth A], C [auth A], D [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| 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: 1.55 Å
- R-Value Free: 0.212
- R-Value Work: 0.179
- R-Value Observed: 0.181
- Space Group: P 41 21 2
- Diffraction Data: https://doi.org/10.18430/M32QML
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 80.78 | α = 90 |
| b = 80.78 | β = 90 |
| c = 70.56 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PHENIX | refinement |
| SHELX | phasing |
| MolProbity | model building |
| XSCALE | data scaling |
| PDB_EXTRACT | data extraction |
| MAR345 | data collection |
| XDS | data reduction |
| SHELXD | phasing |
| autoSHARP | phasing |
Entry History
Deposition Data
- Released Date: 2007-09-04 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2007-09-04
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: 2023-01-25
Changes: Database references, Derived calculations
