Download MendeleySolution structure of the fifth SH3 domain from human KIAA0418 protein
Inoue, K., Kurosaki, C., Yoshida, M., Hayashi, F., Yokoyama, S.To be published.
2EGC
Solution structure of the fifth SH3 domain from human KIAA0418 protein
- PDB DOI: https://doi.org/10.2210/pdb2EGC/pdb
- BMRB: 11194
- Classification: SIGNALING PROTEIN
- Organism(s): Homo sapiens
- Mutation(s): No
- Deposited: 2007-02-28 Released: 2007-08-28
Experimental Data Snapshot
- Method: SOLUTION NMR
- Conformers Calculated: 100
- Conformers Submitted: 20
- Selection Criteria: structures with the least restraint violations,structures with the lowest energy,target function
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 |
| SH3 and PX domain-containing protein 2A | 75 | Homo sapiens | Mutation(s): 0 Gene Names: SH3PXD2A, FISH, KIAA0418, SH3MD1 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q5TCZ1 (Homo sapiens) Explore Q5TCZ1 Go to UniProtKB: Q5TCZ1 | |||||
PHAROS: Q5TCZ1 GTEx: ENSG00000107957 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q5TCZ1 | ||||
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 least restraint violations,structures with the lowest energy,target function
Entry History
Deposition Data
- Released Date: 2007-08-28 Deposition Author(s): Inoue, K., Kurosaki, C., Yoshida, M., Hayashi, F., Yokoyama, S., RIKEN Structural Genomics/Proteomics Initiative (RSGI)
Revision History (Full details and data files)
- Version 1.0: 2007-08-28
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2022-03-09
Changes: Data collection, Database references, Derived calculations
