Download MendeleySolution structure of the Rhodanese-like domain in human ubiquitin specific protease 8 (UBP8)
Saito, K., Koshiba, S., Inoue, M., Kigawa, T., Yokoyama, S.To be published.
1WHB | pdb_00001whb
Solution structure of the Rhodanese-like domain in human ubiquitin specific protease 8 (UBP8)
- PDB DOI: https://doi.org/10.2210/pdb1WHB/pdb
- Classification: HYDROLASE
- Organism(s): Homo sapiens
- Mutation(s): No
- Deposited: 2004-05-28 Released: 2004-11-28
Experimental Data Snapshot
- Method: SOLUTION NMR
- Conformers Calculated: 100
- Conformers Submitted: 20
- Selection Criteria: structures with the lowest energy
wwPDB Validation 3D Report Full Report
This is version 1.4 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 |
| KIAA0055 | 157 | Homo sapiens | Mutation(s): 0 Gene Names: Kazusa cDNA ha01049 EC: 3.1.2.15 (PDB Primary Data), 3.4.19.12 (UniProt) |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P40818 (Homo sapiens) Explore P40818 Go to UniProtKB: P40818 | |||||
PHAROS: P40818 GTEx: ENSG00000138592 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P40818 | ||||
Sequence AnnotationsExpand | |||||
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Experimental Data & Validation
Experimental Data
- Method: SOLUTION NMR
- Conformers Calculated: 100
- Conformers Submitted: 20
- Selection Criteria: structures with the lowest energy
Entry History
Deposition Data
- Released Date: 2004-11-28 Deposition Author(s): Saito, K., Koshiba, S., Inoue, M., Kigawa, T., Yokoyama, S., RIKEN Structural Genomics/Proteomics Initiative (RSGI)
Revision History (Full details and data files)
- Version 1.0: 2004-11-28
Type: Initial release - Version 1.1: 2008-04-30
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 1.3: 2022-03-02
Changes: Data collection, Database references, Derived calculations - Version 1.4: 2024-05-29
Changes: Data collection
