Download MendeleyCrystal structure of a Function Uncharacterized Domain of E3 Ubiquitin Ligase SHPRH
Zhang, Q., Dong, A., Li, Y., Walker, J.R., Guan, X., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Tong, Y.To be published.
4QN1
Crystal Structure of a Functionally Uncharacterized Domain of E3 Ubiquitin Ligase SHPRH
- PDB DOI: https://doi.org/10.2210/pdb4QN1/pdb
- Classification: UNKNOWN FUNCTION
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2014-06-17 Released: 2014-08-13
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.48 Å
- R-Value Free: 0.257
- R-Value Work: 0.226
- R-Value Observed: 0.227
wwPDB Validation 3D Report Full Report
This is version 1.2 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 |
| E3 ubiquitin-protein ligase SHPRH | 420 | Homo sapiens | Mutation(s): 0 Gene Names: SHPRH, KIAA2023 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q149N8 (Homo sapiens) Explore Q149N8 Go to UniProtKB: Q149N8 | |||||
PHAROS: Q149N8 GTEx: ENSG00000146414 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q149N8 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| SO4 Query on SO4 | C [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| ZN Query on ZN | B [auth A] | ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N |  | ||
| UNX Query on UNX | D [auth A] | UNKNOWN ATOM OR ION X |  | ||
| 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: 2.48 Å
- R-Value Free: 0.257
- R-Value Work: 0.226
- R-Value Observed: 0.227
- Space Group: P 61 2 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 130.624 | α = 90 |
| b = 130.624 | β = 90 |
| c = 129.571 | γ = 120 |
| Software Name | Purpose |
|---|---|
| DENZO | data reduction |
| SCALEPACK | data scaling |
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| SBC-Collect | data collection |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| SOLVE | phasing |
| BUSTER | refinement |
Entry History
Deposition Data
- Released Date: 2014-08-13 Deposition Author(s): Dong, A., Zhang, Q., Li, Y., Walker, J.R., Guan, X., Bountra, C., Arrowsmith, C.H., Edwards, A.M., Tong, Y., Structural Genomics Consortium (SGC)
Revision History (Full details and data files)
- Version 1.0: 2014-08-13
Type: Initial release - Version 1.1: 2014-12-03
Changes: Structure summary - Version 1.2: 2017-11-22
Changes: Refinement description
