3h3g

Crystal structure of the extracellular domain of the human parathyroid hormone receptor (PTH1R) in complex with parathyroid hormone-related protein (PTHrP)

Method: X-RAY DIFFRACTION Dmax: 97.9 Å Quality: GOOD

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

Fusion protein of Maltose-binding periplasmic domain and human parathyroid hormone receptor extracellular domain

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 Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 26–392 Fragment:extracellular domain Parathyroid hormone-related protein × 1 (P12272) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;298 K;7.5% PEG 2000, 13% PEG 400, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 1.94 Å R-free 0.233

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 Maltose-binding periplasmic domain and human parathyroid hormone receptor extracellular domain

Homo sapiens

UniProt Q03431

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 Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 29–187 Fragment:extracellular domain Parathyroid hormone-related protein × 1 (P12272) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;298 K;7.5% PEG 2000, 13% PEG 400, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 1.94 Å R-free 0.233

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.

43 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTH1R_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 375–533; UniProt 29–187

Parathyroid hormone-related protein

OrganismNot specified

UniProt P12272

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 Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 48–70 Fragment:residues 12-34 Non-standard monomer:Yes (specific site not provided by mmCIF) Fusion protein of Maltose-binding periplasmic domain and human parathyroid hormone receptor extracellular domain × 1 (P0AEX9,Q03431) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;298 K;7.5% PEG 2000, 13% PEG 400, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 1.94 Å R-free 0.233

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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTHR_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–23; UniProt 48–70

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 3h3g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3h3g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3h3g
Deposition date deposition_date2009-04-16
Structure title titleCrystal structure of the extracellular domain of the human parathyroid hormone receptor (PTH1R) in complex with parathyroid hormone-related protein (PTHrP)
Keywords keywordsGPCR, extracellular domain, PTHrP, PTH, PTHR1, Sugar transport, Transport, Hormone, 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_guinier28.81
Radius of gyration Rg (electron density) rg_electron28.13
Forward intensity I(0) i048493800.00
Molecular weight molecular_weight55366.0 kDa
Excluded volume excluded_volume69735 ų
Envelope volume envelope_volume87268 ų
Hydration-shell volume shell_volume27470 ų
Envelope diameter envelope_diameter104.9
Shell Rg shell_rg33.10
Envelope Rg envelope_rg28.56
Shape Rg shape_rg28.09
Total Rg total_rg28.78
Total atoms total_atoms3912
Residues n_residues493
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 dmax97.9
Rg (real space) rg_real28.98
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real4.8490e+07
I(0) uncertainty (real space) i0_real_error7.8360e+05
Rg (reciprocal space) rg_reciprocal28.91
I(0) (reciprocal space) i0_reciprocal48490000.0000
Solution quality estimate total_estimate0.8549
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.7
Skewness Skewness skewness0.476
Kurtosis Kurtosis kurtosis-0.392
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10850000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.791; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.767; Smooth: 0.970

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id3h3gA01
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_id3h3gA02
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_id3h3gA03
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)