Download MendeleyCrystal Structure of the C-terminal Phophotyrosine Interaction Domain of Human APBB3
Saijo, S., Nishino, A., Kishishita, S., Shirouzu, M., Yokoyama, S.To be published.
2DYQ | pdb_00002dyq
Crystal Structure of the C-terminal Phophotyrosine Interaction Domain of Human APBB3
- PDB DOI: https://doi.org/10.2210/pdb2DYQ/pdb
- Classification: PROTEIN BINDING
- Organism(s): Homo sapiens
- Mutation(s): No
- Deposited: 2006-09-16 Released: 2007-09-18
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 3.10 Å
- R-Value Free: 0.298 (Depositor), 0.270 (DCC)
- R-Value Work: 0.254 (Depositor), 0.246 (DCC)
- R-Value Observed: 0.256 (Depositor)
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 |
| Amyloid beta A4 precursor protein-binding family B member 3 | 144 | Homo sapiens | Mutation(s): 0 Gene Names: APBB3, FE65L2 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for O95704 (Homo sapiens) Explore O95704 Go to UniProtKB: O95704 | |||||
GTEx: ENSG00000113108 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | O95704 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| 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: 3.10 Å
- R-Value Free: 0.298 (Depositor), 0.270 (DCC)
- R-Value Work: 0.254 (Depositor), 0.246 (DCC)
- R-Value Observed: 0.256 (Depositor)
Space Group: P 62 2 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 82.292 | α = 90 |
| b = 82.292 | β = 90 |
| c = 104.871 | γ = 120 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| HKL-2000 | data collection |
| HKL-2000 | data reduction |
| SCALEPACK | data scaling |
| SOLVE | phasing |
Entry History
Deposition Data
- Released Date: 2007-09-18 Deposition Author(s): Nishino, A., Saijo, S., Kishishita, S., Shirouzu, M., Yokoyama, S., RIKEN Structural Genomics/Proteomics Initiative (RSGI)
Revision History (Full details and data files)
- Version 1.0: 2007-09-18
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.2: 2024-10-30
Changes: Data collection, Database references, Derived calculations, Structure summary
