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5ohd

Putative inactive (dormant) dimeric state of GHR transmembrane domain

Method: SOLUTION NMR Dmax: 83.0 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Growth hormone receptor

Homo sapiens

UniProt P10912

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 254–294 Chain B； UniProt 254–294 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 5；313 K；Ionic strength (raw mmCIF value) 40；Pressure AMBIENT NMR sample composition：0.7 mM [U-99% 13C; U-99% 15N] GHRtm, 1.2 mM GHRtm, 100 mM [U-99% 2H] DPC, 0.3 mM sodium azide, 8 mM TCEP, 10 mM citric acid, 20 mM Na2HPO4, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition：0.8 mM [U-99% 15N] GHRtm, 50 mM [U-99% 2H] DPC, 0.3 mM sodium azide, 8 mM TCEP, 10 mM citric acid, 20 mM Na2HPO4, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition：0.8 mM [U-99% 13C; U-99% 15N] GHRtm, 50 mM [U-99% 2H] DPC, 0.3 mM sodium azide, 8 mM TCEP, 10 mM citric acid, 20 mM Na2HPO4, 95% H2O/5% D2O | 95% H2O/5% D2O Resolution not provided

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.

Other PDB Difference from Current Entry 5OHD Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1A22 HUMAN GROWTH HORMONE BOUND TO SINGLE RECEPTOR Deposited 1998-01-15 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 19–256（238 aa） Fragment：EXTRACELLULAR DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.5
Resolution 2.60 Å
1A22 HUMAN GROWTH HORMONE BOUND TO SINGLE RECEPTOR Deposited 1998-01-15 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 19–256（238 aa） Fragment：EXTRACELLULAR DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.5
Resolution 2.60 Å
1AXI STRUCTURAL PLASTICITY AT THE HGH:HGHBP INTERFACE Deposited 1997-10-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 19–254（236 aa） Fragment：EXTRACELLULAR BINDING DOMAIN
Mutation：W104A SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions streak seeding；pH 6.5；CRYSTALLIZED BY STREAK SEEDING AT 5MG/ML COMPLEX IN 50MM BIS-TRIS (PH 6.5) 20% SATURATED AMMONIUM SULFATE, streak seeding
Resolution 2.10 Å R-free 0.262
1HWG 1:2 COMPLEX OF HUMAN GROWTH HORMONE WITH ITS SOLUBLE BINDING PROTEIN Deposited 1996-11-13 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 19–255（237 aa） Fragment：EXTRACELLULAR DOMAIN
Chain C 19–255（237 aa） Fragment：EXTRACELLULAR DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；THE PROTEIN COMPLEX WAS CRYSTALLISED AT PH 6.5 USING 45% (W/V) LISO4 WITH 2% PEG-500 DME AND SOAKED TO PH 5.5 PRIOR TO DATA COLLECTION
Resolution 2.50 Å R-free 0.287
1HWH 1:1 COMPLEX OF HUMAN GROWTH HORMONE MUTANT G120R WITH ITS SOLUBLE BINDING PROTEIN Deposited 1996-11-13 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 19–255（237 aa） Fragment：EXTRACELLULAR DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.75；THE PROTEIN COMPLEX WAS CRYSTALLISED FROM 1.6 M LISO4 AND 50 MM BIS TRIS AT PH 6.75
Resolution 2.90 Å R-free 0.317
1KF9 PHAGE DISPLAY DERIVED VARIANT OF HUMAN GROWTH HORMONE COMPLEXED WITH TWO COPIES OF THE EXTRACELLULAR DOMAIN OF ITS RECEPTOR Deposited 2001-11-19 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 19–256（238 aa）
Chain C 19–256（238 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.3；pH 6.30
Resolution 2.60 Å R-free 0.326
1KF9 PHAGE DISPLAY DERIVED VARIANT OF HUMAN GROWTH HORMONE COMPLEXED WITH TWO COPIES OF THE EXTRACELLULAR DOMAIN OF ITS RECEPTOR Deposited 2001-11-19 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain E 19–256（238 aa）
Chain F 19–256（238 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.3；pH 6.30
Resolution 2.60 Å R-free 0.326
2AEW A model for growth hormone receptor activation based on subunit rotation within a receptor dimer Deposited 2005-07-24 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 47–251（205 aa） Fragment：residues 29-233
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；283 K；PEG, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 283K
Resolution 2.70 Å R-free 0.302
2AEW A model for growth hormone receptor activation based on subunit rotation within a receptor dimer Deposited 2005-07-24 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 47–251（205 aa） Fragment：residues 29-233
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；283 K；PEG, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 283K
Resolution 2.70 Å R-free 0.302
3HHR HUMAN GROWTH HORMONE AND EXTRACELLULAR DOMAIN OF ITS RECEPTOR: CRYSTAL STRUCTURE OF THE COMPLEX Deposited 1993-12-30 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 50–255（206 aa）
Chain C 50–254（205 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.80 Å
5OEK Putative active dimeric state of GHR transmembrane domain Deposited 2017-07-08 Parsed fields agree Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 254–294（41 aa）
Chain B 254–294（41 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5；313 K；Ionic strength (raw mmCIF value) 40；Pressure AMBIENT
NMR sample composition 0.7 mM [U-99% 13C; U-99% 15N] GHRtm, 1.2 mM GHRtm, 100 mM [U-99% 2H] DPC, 0.3 mM sodium azide, 8 mM TCEP, 10 mM citric acid, 20 mM Na2HPO4, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 0.8 mM [U-99% 15N] GHRtm, 50 mM [U-99% 2H] DPC, 0.3 mM sodium azide, 8 mM TCEP, 10 mM citric acid, 20 mM Na2HPO4, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 0.8 mM [U-99% 13C; U-99% 15N] GHRtm, 50 mM [U-99% 2H] DPC, 0.3 mM sodium azide, 8 mM TCEP, 10 mM citric acid, 20 mM Na2HPO4, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided

8 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GHR_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 3–43； UniProt 254–294 Author chain B； PDBConstruct 3–43； UniProt 254–294

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 5ohd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5ohd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5ohd
Deposition date deposition_date2017-07-15
Structure title titlePutative inactive (dormant) dimeric state of GHR transmembrane domain
Keywords keywordsDimer, GHR, Growth hormone receptor, Homodimer, Human, Receptor, Transmembrane domain, JAK2 tyrosine kinase, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier22.79 Å
Radius of gyration Rg (electron density) rg_electron20.91 Å
Forward intensity I(0) i0418641000.00
Molecular weight molecular_weight205010.0 kDa
Excluded volume excluded_volume269060 ų
Envelope volume envelope_volume77680 ų
Hydration-shell volume shell_volume23720 ų
Envelope diameter envelope_diameter85.3 Å
Shell Rg shell_rg34.52 Å
Envelope Rg envelope_rg27.81 Å
Shape Rg shape_rg20.79 Å
Total Rg total_rg21.96 Å
Total atoms total_atoms29160
Residues n_residues1720
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax83.0 Å
Rg (real space) rg_real22.98 Å
Rg uncertainty (real space) rg_real_error1.20 Å
I(0) (real space) i0_real4.1860e+08
I(0) uncertainty (real space) i0_real_error7.0470e+06
Rg (reciprocal space) rg_reciprocal22.94 Å
I(0) (reciprocal space) i0_reciprocal418600000.0000
Solution quality estimate total_estimate0.7779
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary18.9 Å
Skewness Skewness skewness0.331
Kurtosis Kurtosis kurtosis-0.559
Angular range angular_range— – 0.3500 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha119800.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.511; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.590; Smooth: 0.995
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (2)

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9. Files and Curves (10)