Download MendeleySolution structure of the third ig-like domain from human Advanced glycosylation end product-specific receptor
Wakabayashi, M., Kurosaki, C., Yoshida, M., Hayashi, F., Yokoyama, S.To be published.
2ENS
Solution structure of the third ig-like domain from human Advanced glycosylation end product-specific receptor
- PDB DOI: https://doi.org/10.2210/pdb2ENS/pdb
- Classification: SIGNALING PROTEIN
- Organism(s): Homo sapiens
- Mutation(s): No
- Deposited: 2007-03-28 Released: 2008-04-01
Experimental Data Snapshot
- Method: SOLUTION NMR
- Conformers Calculated: 100
- Conformers Submitted: 20
- Selection Criteria: structures with the least restraint violations, target function
wwPDB Validation 3D Report Full Report
This is version 1.2 of the entry. See complete history.
Literature
To be published.
Macromolecules
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(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Advanced glycosylation end product-specific receptor | 96 | Homo sapiens | Mutation(s): 0 Gene Names: AGER |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q15109 (Homo sapiens) Explore Q15109 Go to UniProtKB: Q15109 | |||||
PHAROS: Q15109 GTEx: ENSG00000204305 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q15109 | ||||
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, target function
Entry History
Deposition Data
- Released Date: 2008-04-01 Deposition Author(s): Wakabayashi, M., Kurosaki, C., Yoshida, M., Hayashi, F., Yokoyama, S., RIKEN Structural Genomics/Proteomics Initiative (RSGI)
Revision History (Full details and data files)
- Version 1.0: 2008-04-01
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
