Download MendeleyCrystal structure of the 32th Ig-like domain of human obscurin (KIAA1556)
Saijo, S., Ohsawa, N., Nishino, A., Kishishita, S., Chen, L., Fu, Z.Q., Chrzas, J., Wang, B.C., Shirouzu, M., Yokoyama, S.To be published.
2YZ8 | pdb_00002yz8
Crystal structure of the 32th Ig-like domain of human obscurin (KIAA1556)
- PDB DOI: https://doi.org/10.2210/pdb2YZ8/pdb
- Classification: STRUCTURAL PROTEIN
- Organism(s): Homo sapiens
- Mutation(s): No
- Deposited: 2007-05-04 Released: 2008-05-06
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.00 Å
- R-Value Free: 0.261 (Depositor), 0.220 (DCC)
- R-Value Work: 0.209 (Depositor), 0.210 (DCC)
- R-Value Observed: 0.214 (Depositor)
Starting Model: in silico
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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 |
| Obscurin | 103 | Homo sapiens | Mutation(s): 0 Gene Names: OBSCN, KIAA1556 EC: 2.7.11.1 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q5VST9 (Homo sapiens) Explore Q5VST9 Go to UniProtKB: Q5VST9 | |||||
PHAROS: Q5VST9 GTEx: ENSG00000154358 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q5VST9 | ||||
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: 2.00 Å
- R-Value Free: 0.261 (Depositor), 0.220 (DCC)
- R-Value Work: 0.209 (Depositor), 0.210 (DCC)
- R-Value Observed: 0.214 (Depositor)
Space Group: P 43 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 43.358 | α = 90 |
| b = 43.358 | β = 90 |
| c = 102.316 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| HKL-2000 | data collection |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| MOLREP | phasing |
Entry History
Deposition Data
- Released Date: 2008-05-06 Deposition Author(s): Saijo, S., Ohsawa, N., Nishino, A., Kishishita, S., Chen, L., Fu, Z.Q., Chrzas, J., Wang, B.C., Shirouzu, M., Yokoyama, S., RIKEN Structural Genomics/Proteomics Initiative (RSGI)
Revision History (Full details and data files)
- Version 1.0: 2008-05-06
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.2: 2024-04-03
Changes: Data collection, Database references, Derived calculations, Refinement description - Version 1.3: 2024-11-13
Changes: Structure summary
