Download MendeleyStructure and interaction mode of the UBX-L domain of VCIP135 determined by solution NMR spectroscopy
Iwazu, T., Murayama, S., Igarashi, R., Hrioaki, H., Shirakawa, M., Tochio, H.To be published.
2MX2 | pdb_00002mx2
UBX-L domain of VCIP135
- PDB DOI: https://doi.org/10.2210/pdb2MX2/pdb
- BMRB: 25382
- Classification: HYDROLASE
- Organism(s): Rattus norvegicus
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2014-12-07 Released: 2016-07-13
Experimental Data Snapshot
- Method: SOLUTION NMR
- Conformers Calculated: 200
- Conformers Submitted: 20
- Selection Criteria: structures with the least restraint violations
wwPDB Validation 3D Report Full Report
This is version 2.0 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 |
| Deubiquitinating protein VCIP135 | 86 | Rattus norvegicus | Mutation(s): 0 Gene Names: Vcpip1, Vcip135 EC: 3.4.19.12 |  | |
UniProt | |||||
Find proteins for Q8CF97 (Rattus norvegicus) Explore Q8CF97 Go to UniProtKB: Q8CF97 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q8CF97 | ||||
Sequence AnnotationsExpand | |||||
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Experimental Data & Validation
Experimental Data
- Method: SOLUTION NMR
- Conformers Calculated: 200
- Conformers Submitted: 20
- Selection Criteria: structures with the least restraint violations
Entry History
Deposition Data
- Released Date: 2016-07-13 Deposition Author(s): Iwazu, T., Murayama, S., Igarashi, R., Hrioaki, H., Shirakawa, M., Tochio, H.
Revision History (Full details and data files)
- Version 1.0: 2016-07-13
Type: Initial release - Version 2.0: 2024-05-01
Changes: Advisory, Atomic model, Data collection, Database references, Derived calculations, Polymer sequence, Source and taxonomy, Structure summary
