3O3U
Crystal Structure of Human Receptor for Advanced Glycation Endproducts (RAGE)
- PDB DOI: https://doi.org/10.2210/pdb3O3U/pdb
- Classification: TRANSPORT PROTEIN, SIGNALING PROTEIN
- Organism(s): Escherichia coli, Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): No 
- Deposited: 2010-07-26 Released: 2010-10-13 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.50 Å
- R-Value Free: 0.184 
- R-Value Work: 0.168 
- R-Value Observed: 0.169 
wwPDB Validation   3D Report Full Report
This is version 2.0 of the entry. See complete history. 
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
Maltose-binding periplasmic protein, Advanced glycosylation end product-specific receptor | A [auth N] | 581 | Escherichia coli, Homo sapiens This entity is chimeric | Mutation(s): 0  Gene Names: b4034, JW3994, malE, rage, AGER | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P0AEX9 (Escherichia coli (strain K12)) Explore P0AEX9  Go to UniProtKB:  P0AEX9 | |||||
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 Groups | Q15109P0AEX9 | ||||
Sequence AnnotationsExpand | |||||
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Oligosaccharides
Small Molecules
Ligands 1 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
SO4 Query on SO4 | C [auth N] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |
Biologically Interesting Molecules (External Reference) 1 Unique
Entity ID: 2 | |||||
---|---|---|---|---|---|
ID | Chains | Name | Type/Class | 2D Diagram | 3D Interactions |
PRD_900009 Query on PRD_900009 | B [auth A] | alpha-maltotriose | Oligosaccharide / Nutrient |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.50 Å
- R-Value Free: 0.184 
- R-Value Work: 0.168 
- R-Value Observed: 0.169 
- Space Group: P 21 21 2
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 81.739 | α = 90 |
b = 89.308 | β = 90 |
c = 97.978 | γ = 90 |
Software Name | Purpose |
---|---|
SERGUI | data collection |
MOLREP | phasing |
PHENIX | refinement |
HKL-2000 | data reduction |
HKL-2000 | data scaling |
Entry History 
Deposition Data
- Released Date: 2010-10-13  Deposition Author(s): Park, H., Boyington, J.C.
Revision History (Full details and data files)
- Version 1.0: 2010-10-13
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2017-08-02
Changes: Advisory, Refinement description, Source and taxonomy - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Atomic model, Data collection, Database references, Derived calculations, Non-polymer description, Structure summary