Download MendeleyCrystal structure of a RNA binding domain of Hypothetical POLYADENYLATE-BINDING PROTEIN (PABPN1) from Homo sapiens at 1.95 A resolution
Joint Center for Structural Genomics (JCSG), Partnership for T-Cell BiologyTo be published.
3UCG
Crystal structure of a RNA binding domain of polyadenylate-binding protein (PABPN1) from Homo sapiens at 1.95 A resolution
- PDB DOI: https://doi.org/10.2210/pdb3UCG/pdb
- Classification: RNA BINDING PROTEIN
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2011-10-26 Released: 2011-11-23
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.95 Å
- R-Value Free: 0.210
- R-Value Work: 0.163
- R-Value Observed: 0.165
wwPDB Validation 3D Report Full Report
This is version 1.5 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 |
| Polyadenylate-binding protein 2 | 89 | Homo sapiens | Mutation(s): 0 Gene Names: BC010939, PAB2, PABP2, PABPN1 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q86U42 (Homo sapiens) Explore Q86U42 Go to UniProtKB: Q86U42 | |||||
PHAROS: Q86U42 GTEx: ENSG00000100836 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q86U42 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PGE Query on PGE | F [auth A] | TRIETHYLENE GLYCOL C6 H14 O4 ZIBGPFATKBEMQZ-UHFFFAOYSA-N |  | ||
| PEG Query on PEG | E [auth A] | DI(HYDROXYETHYL)ETHER C4 H10 O3 MTHSVFCYNBDYFN-UHFFFAOYSA-N |  | ||
| SO4 Query on SO4 | B [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| EDO Query on EDO | C [auth A], D [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: 1.95 Å
- R-Value Free: 0.210
- R-Value Work: 0.163
- R-Value Observed: 0.165
- Space Group: I 2 3
- Diffraction Data: https://doi.org/10.18430/M33UCG
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 92.678 | α = 90 |
| b = 92.678 | β = 90 |
| c = 92.678 | γ = 90 |
| Software Name | Purpose |
|---|---|
| MolProbity | model building |
| PDB_EXTRACT | data extraction |
| SHELX | phasing |
| SHARP | phasing |
| XSCALE | data scaling |
| REFMAC | refinement |
| XDS | data reduction |
| SHELXD | phasing |
Entry History
Deposition Data
- Released Date: 2011-11-23 Deposition Author(s): Joint Center for Structural Genomics (JCSG), Partnership for T-Cell Biology (TCELL)
Revision History (Full details and data files)
- Version 1.0: 2011-11-23
Type: Initial release - Version 1.1: 2012-08-29
Changes: Structure summary - Version 1.2: 2014-12-24
Changes: Structure summary - Version 1.3: 2017-11-08
Changes: Refinement description - Version 1.4: 2018-01-24
Changes: Database references - Version 1.5: 2023-02-01
Changes: Database references, Derived calculations
