SAXSdb — 1bzg

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

PARATHYROID HORMONE-RELATED PROTEIN

Homo sapiens

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 37–70	Fragment：RESIDUES 1-34	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 5.1；277 K；Ionic strength (raw mmCIF value) 550mM；Pressure 10E+5PA NMR sample composition：H2O/D2O (9:1)	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 1BZG	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1M5N Crystal structure of HEAT repeats (1-11) of importin b bound to the non-classical NLS(67-94) of PTHrP Deposited 2002-07-09	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain Q 103–130（28 aa） Fragment：Residues 67-94	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；298 K；MES, PEG 4000, sodium chloride, Tween, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K, pH 6.00	Resolution 2.90 Å R-free 0.297
3FFD Structure of parathyroid hormone-related protein complexed to a neutralizing monoclonal antibody Deposited 2008-12-03	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 P 37–144（108 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.7；295 K；PEG 400, TRIS, pH 8.70, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.00 Å R-free 0.271
3H3G Crystal structure of the extracellular domain of the human parathyroid hormone receptor (PTH1R) in complex with parathyroid hormone-related protein (PTHrP) Deposited 2009-04-16	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 48–70（23 aa） Fragment：residues 12-34	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	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
7UZO Parathyroid hormone 1 receptor extracellular domain complexed with a peptide ligand containing one beta-amino acid Deposited 2022-05-09	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 × 2 PDB declaration: dimeric	Chain B 51–72（22 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；28 % v/v PEG Smear Low, 0.1 M tris-HCl pH 8, 0.15 M Sodium citrate, 1% ethylene glycol, 0.4 mM ZnSO4	Resolution 1.30 Å R-free 0.182
7VVJ PTHrP-bound human PTH1R in complex with Gs Deposited 2021-11-06	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain P 37–72（36 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
8D51 Parathyroid hormone 1 receptor extracellular domain complexed with a peptide ligand containing beta-3-homotryptophan Deposited 2022-06-03	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 × 2 PDB declaration: dimeric	Chain B 51–72（22 aa）	Mutation：I31 substituted with beta-3-tryptophan Non-standard monomer：Yes (specific site not provided by mmCIF)	EDO 1,2-ETHANEDIOL × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；28 % v/v PEG Smear Low, 0.1 M tris-HCl pH 8, 0.15 M Sodium citrate, 1% ethylene glycol, 1 mM ZnSO4	Resolution 2.00 Å R-free 0.246
8D52 Parathyroid hormone 1 receptor extracellular domain complexed with a peptide ligand containing (2-naphthyl)-beta-3-homoalanine Deposited 2022-06-03	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 × 2 PDB declaration: dimeric	Chain B 51–72（22 aa）	Mutation：I31 substituted by (2-naphthyl)-beta-3-homoalanine Non-standard monomer：Yes (specific site not provided by mmCIF)	EDO 1,2-ETHANEDIOL × 1 ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；293 K；28 % v/v PEG Smear Low, 0.1 M tris-HCl pH 8, 0.15 M Sodium citrate, 1% ethylene glycol, 1 mM ZnSO4	Resolution 2.02 Å R-free 0.244
8FLR Human PTH1R in complex with PTHrP and Gs Deposited 2022-12-22	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain P 37–72（36 aa） Fragment：UNP residues 37-72	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4；Buffer also contained 2 micromolar PTHrP peptide. cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.94 Å
8HAF PTHrP-PTH1R-Gs complex Deposited 2022-10-26	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 × 6 PDB declaration: hexameric	Chain P 37–72（36 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	PLM PALMITIC ACID × 11 CLR CHOLESTEROL × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.25 Å

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	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–34； UniProt 37–70

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1bzg
Deposition date deposition_date	1998-10-28
Structure title title	THE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE-RELATED PROTEIN (1-34) IN NEAR-PHYSIOLOGICAL SOLUTION, NMR, 30 STRUCTURES
Keywords keywords	;HUMAN PEPTIDE HORMONE, STIMULATING INTRACELLULAR CAMP FORMATION, SERUM CALCIUM LEVEL, HUMORAL HYPERCALCEMIA OF MALIGNANCY, SOLUTION STRUCTURE, PTHRP, PTH, HORMONE ;; HORMONE
Experimental Method method	SOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier	13.37 Å
Radius of gyration Rg (electron density) rg_electron	13.45 Å
Forward intensity I(0) i0	212129000.00
Molecular weight molecular_weight	120560.0 kDa
Excluded volume excluded_volume	150800 Å³
Envelope volume envelope_volume	31072 Å³
Hydration-shell volume shell_volume	14917 Å³
Envelope diameter envelope_diameter	63.9 Å
Shell Rg shell_rg	23.46 Å
Envelope Rg envelope_rg	18.37 Å
Shape Rg shape_rg	13.42 Å
Total Rg total_rg	13.95 Å
Total atoms total_atoms	17190
Residues n_residues	1020
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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

Maximum dimension Dmax dmax	57.3 Å
Rg (real space) rg_real	13.55 Å
Rg uncertainty (real space) rg_real_error	0.72 Å
I(0) (real space) i0_real	2.1210e+08
I(0) uncertainty (real space) i0_real_error	2.3520e+06
Rg (reciprocal space) rg_reciprocal	13.54 Å
I(0) (reciprocal space) i0_reciprocal	212100000.0000
Solution quality estimate total_estimate	0.7042
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	4
Primary peak position r_peak_primary	16.7 Å
Skewness Skewness skewness	0.477
Kurtosis Kurtosis kurtosis	-0.258
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	20620.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.360; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.076; 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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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1bzga_
Class class	j — Peptides
Fold Fold fold	j.15 — Parathyroid hormone fragments (residues between 1 and 39)
Superfamily Superfamily superfamily	j.15.1 — Parathyroid hormone fragments (residues between 1 and 39)
Family Family family	j.15.1.1 — Parathyroid hormone fragments (residues between 1 and 39)

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	1

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Description description	PARATHYROID HORMONE-RELATED PROTEIN
Molecular weight formula_weight	4027.6 kDa
Source method src_method	man
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	17190

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606

THE SOLUTION STRUCTURE OF HUMAN PARATHYROID HORMONE-RELATED PROTEIN (1-34) IN NEAR-PHYSIOLOGICAL SOLUTION, NMR, 30 STRUCTURES

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

PARATHYROID HORMONE-RELATED PROTEIN

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/bz/1bzg/1bzg.fit
pddf	/app/data/pr_computation/bz/1bzg/1bzg.pr.out
profile	/app/data/saxs_computation/bz/1bzg/1bzg.dat