3ehs

Crystal structure of the extracellular domain of human corticotropin releasing factor receptor type 1 (CRFR1)

Method: X-RAY DIFFRACTION Dmax: 82.3 Å Quality: EXCELLENT

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

fusion protein of CRFR1 extracellular domain and MBP

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 A; UniProt 26–392 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 4.7;293 K;NaCl, sucrose, sodium acetate, pH 4.7, vapor diffusion, temperature 293K Resolution 2.76 Å R-free 0.240

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 A; PDBConstruct 2–368; UniProt 26–392

fusion protein of CRFR1 extracellular domain and MBP

Homo sapiens

UniProt P34998

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 A; UniProt 24–119 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 4.7;293 K;NaCl, sucrose, sodium acetate, pH 4.7, vapor diffusion, temperature 293K Resolution 2.76 Å R-free 0.240

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.

7 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CRFR1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 375–470; UniProt 24–119

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 3ehs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3ehs
Deposition date deposition_date2008-09-14
Structure title titleCrystal structure of the extracellular domain of human corticotropin releasing factor receptor type 1 (CRFR1)
Keywords keywords;G protein-coupled receptor, corticotropin releasing factor, SCR fold, MBP fusion, extracellular domain, Sugar transport, Transport, Cell membrane, Glycoprotein, Membrane, Phosphoprotein, Receptor, Transducer, Transmembrane, MEMBRANE PROTEIN ;; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.55
Radius of gyration Rg (electron density) rg_electron25.53
Forward intensity I(0) i041648400.00
Molecular weight molecular_weight50467.0 kDa
Excluded volume excluded_volume63392 ų
Envelope volume envelope_volume82613 ų
Hydration-shell volume shell_volume27671 ų
Envelope diameter envelope_diameter85.2
Shell Rg shell_rg31.99
Envelope Rg envelope_rg25.76
Shape Rg shape_rg25.49
Total Rg total_rg26.43
Total atoms total_atoms3562
Residues n_residues457
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 dmax82.3
Rg (real space) rg_real26.54
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real4.1650e+07
I(0) uncertainty (real space) i0_real_error6.0670e+05
Rg (reciprocal space) rg_reciprocal26.54
I(0) (reciprocal space) i0_reciprocal41650000.0000
Solution quality estimate total_estimate0.9104
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.8
Skewness Skewness skewness0.285
Kurtosis Kurtosis kurtosis-0.556
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5044000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.963; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.955

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id3ehsA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id3ehsA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id3ehsA03
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology1240 — Hormone receptor fold
Homologous superfamily homologous superfamily10 — GPCR, family 2, extracellular hormone receptor domain

8. Citations (1)

9. Files and Curves (10)