Download MendeleyCrystal structure of a Putative Sel1 repeat protein (KPN_04481) from Klebsiella pneumoniae subsp. pneumoniae MGH 78578 at 1.65 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
3RJV
Crystal structure of a putative sel1 repeat protein (kpn_04481) from Klebsiella pneumoniae subsp. pneumoniae at 1.65 a resolution
- PDB DOI: https://doi.org/10.2210/pdb3RJV/pdb
- Classification: PROTEIN BINDING
- Organism(s): Klebsiella pneumoniae subsp. pneumoniae MGH 78578
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2011-04-15 Released: 2011-05-04
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.65 Å
- R-Value Free: 0.194
- R-Value Work: 0.171
- R-Value Observed: 0.172
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 |
| Putative Sel1 repeat protein | 212 | Klebsiella pneumoniae subsp. pneumoniae MGH 78578 | Mutation(s): 0 Gene Names: yjcO, KPN78578_44120, KPN_04481 |  | |
UniProt | |||||
Find proteins for A6TH02 (Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)) Explore A6TH02 Go to UniProtKB: A6TH02 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A6TH02 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| EDO Query on EDO | B [auth A] C [auth A] D [auth A] E [auth A] F [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-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: 1.65 Å
- R-Value Free: 0.194
- R-Value Work: 0.171
- R-Value Observed: 0.172
- Space Group: P 31 2 1
- Diffraction Data: https://doi.org/10.18430/M33RJV
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 81.508 | α = 90 |
| b = 81.508 | β = 90 |
| c = 83.343 | γ = 120 |
| Software Name | Purpose |
|---|---|
| MolProbity | model building |
| PDB_EXTRACT | data extraction |
| SHELX | phasing |
| SHARP | phasing |
| SCALA | data scaling |
| REFMAC | refinement |
| MOSFLM | data reduction |
| SHELXD | phasing |
Entry History
Deposition Data
- Released Date: 2011-05-04 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2011-05-04
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2017-11-08
Changes: Refinement description - Version 1.3: 2023-02-01
Changes: Database references, Derived calculations
