3o3u

Crystal Structure of Human Receptor for Advanced Glycation Endproducts (RAGE)

Method: X-RAY DIFFRACTION Dmax: 86.3 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

Maltose-binding periplasmic protein, Advanced glycosylation end product-specific receptor

Homo sapiens

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain N; UniProt 28–384 Fragment:MBP: UNP residues 28-384, RAGE: UNP residues 23-231 alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;200 mM Li sulfate, 100 mM Tris-HCl, pH 7.5 and 10% (w/v) polyethylene glycol 4,000 , VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.50 Å R-free 0.184

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain N; PDBConstruct 2–358; UniProt 28–384

Maltose-binding periplasmic protein, Advanced glycosylation end product-specific receptor

Homo sapiens

UniProt Q15109

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain N; UniProt 23–231 Fragment:MBP: UNP residues 28-384, RAGE: UNP residues 23-231 alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;277 K;200 mM Li sulfate, 100 mM Tris-HCl, pH 7.5 and 10% (w/v) polyethylene glycol 4,000 , VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 1.50 Å R-free 0.184

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

31 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAGE_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain N; PDBConstruct 373–581; UniProt 23–231

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 3o3u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3o3u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3o3u
Deposition date deposition_date2010-07-26
Structure title titleCrystal Structure of Human Receptor for Advanced Glycation Endproducts (RAGE)
Keywords keywords;RAGE, AGER, scavenger receptor, macrophage cell surface receptor, innate immune receptor, Ig fold, cell surface receptor, Advanced glycation end products, AGE, Amphoterin, S100B, S100A12, membrane, Sugar transport, Transport, TRANSPORT PROTEIN, SIGNALING PROTEIN ;; TRANSPORT PROTEIN, SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier28.55
Radius of gyration Rg (electron density) rg_electron27.44
Forward intensity I(0) i064903300.00
Molecular weight molecular_weight63816.0 kDa
Excluded volume excluded_volume80295 ų
Envelope volume envelope_volume103330 ų
Hydration-shell volume shell_volume31649 ų
Envelope diameter envelope_diameter91.6
Shell Rg shell_rg34.38
Envelope Rg envelope_rg27.25
Shape Rg shape_rg27.41
Total Rg total_rg28.29
Total atoms total_atoms4503
Residues n_residues580
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax86.3
Rg (real space) rg_real28.37
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real6.4900e+07
I(0) uncertainty (real space) i0_real_error8.3770e+05
Rg (reciprocal space) rg_reciprocal28.43
I(0) (reciprocal space) i0_reciprocal64910000.0000
Solution quality estimate total_estimate0.7385
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.5
Skewness Skewness skewness0.079
Kurtosis Kurtosis kurtosis-0.643
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9424000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.972; Stabil: 1.000; Sysdev: 0.242; Positv: 1.000; Valcen: 0.999; Smooth: 0.953

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id3o3uN02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3o3uN03
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)