SAXSdb — 1hzn

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

CHOLECYSTOKININ TYPE A RECEPTOR

OrganismNot specified

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 329–357	Fragment：RESIDUES 329-357 Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 4.5；303 K；Pressure 1 NMR sample composition：Peptides, DPC	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 1HZN	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1D6G MOLECULAR COMPLEX OF CHOLECYSTOKININ-8 AND N-TERMINUS OF THE CHOLECYSTOKININ A RECEPTOR BY NMR SPECTROSCOPY Deposited 1999-10-13	Different construct Different mutation/modification Different oligomeric state Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–47（47 aa） Fragment：N-TERMINAL DOMAIN (1-47)	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；285 K；Pressure ambient NMR measurement conditions pH 6.5；298 K；Pressure ambient NMR measurement conditions pH 6.5；308 K；Pressure ambient NMR sample composition 1.6mM CCK-A_R(1-47), 171 mM DPC-d38, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1.5mM CCK-8, 137mM DPC-d38, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.8mM CCK-A-R(1-47) + 0.37-3mM CCK-8, 171 mM DPC-d38, 100% D2O \| 100% D2O NMR sample composition 1.6mM CCK-A-R(1-47) + 3mM CCK-8, 171 mM DPC-d38, 100% D2O or 90% H2O, 10% D2O \| 100% D2O or 90% H2O, 10% D2O	Resolution not provided
7EZH Cryo-EM structure of an activated Cholecystokinin A receptor (CCKAR)-Gi complex Deposited 2021-06-01	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain D 1–428（428 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
7EZK Cryo-EM structure of an activated Cholecystokinin A receptor (CCKAR)-Gs complex Deposited 2021-06-01	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain D 1–428（428 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
7EZM Cryo-EM structure of an activated Cholecystokinin A receptor (CCKAR)-Gq complex Deposited 2021-06-01	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain D 1–428（428 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.90 Å
7F8U Crystal structure of the cholecystokinin receptor CCKAR in complex with lintitript Deposited 2021-07-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 37–240（204 aa） Chain A 302–375（74 aa）	Not recorded	1OE 2-[2-[[4-(2-chlorophenyl)-1,3-thiazol-2-yl]carbamoyl]indol-1-yl]ethanoic acid × 1	X-RAY DIFFRACTION X-ray crystallization conditions LIPIDIC CUBIC PHASE；293 K；0.1 M HEPES, pH7.5, 25% PEG400, 250 mM sodium tartrate ,1% 1,2 -butanediol	Resolution 2.80 Å R-free 0.253
7F8X Crystal structure of the cholecystokinin receptor CCKAR in complex with NN9056 Deposited 2021-07-02	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 A 2–240（239 aa） Chain A 302–406（105 aa）	Mutation：F130W,C1251G,C1336A,C1293T,I1376R Mutation：F130W,C1251G,C1336A,C1293T,I1376R	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions LIPIDIC CUBIC PHASE；293 K；100 mM HEPES,7.5, 10 (v/v) PPG400 and 100 mM ammonium acetate	Resolution 3.00 Å R-free 0.261
7F8Y Crystal structure of the cholecystokinin receptor CCKAR in complex with devazepide Deposited 2021-07-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 37–240（204 aa） Chain A 302–406（105 aa）	Mutation：D87N,F130W,R1251G,G1293T,C1336A,I385R Mutation：D87N,F130W,R1251G,G1293T,C1336A,I385R	1OZ N-[(3S)-1-methyl-2-oxidanylidene-5-phenyl-3H-1,4-benzodiazepin-3-yl]-1H-indole-2-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions LIPIDIC CUBIC PHASE；293 K；0.1 M HEPES, pH 7.5, 25% (v/v) PEG400 and 350 mM ammonium acetate	Resolution 2.50 Å R-free 0.268
7MBX Human Cholecystokinin 1 receptor (CCK1R) Gs complex Deposited 2021-04-01	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 R 2–428（427 aa）	Not recorded	Y01 CHOLESTEROL HEMISUCCINATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 1.95 Å
7MBY Human Cholecystokinin 1 receptor (CCK1R) Gq chimera (mGsqi) complex Deposited 2021-04-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 2–428（427 aa）	Not recorded	Y01 CHOLESTEROL HEMISUCCINATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.44 Å
7XOU Structural insights into human brain gut peptide cholecystokinin receptors Deposited 2022-05-01	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain R 1–428（428 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
7XOV Structural insights into human brain gut peptide cholecystokinin receptors Deposited 2022-05-01	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 × 5 PDB declaration: pentameric	Chain R 1–428（428 aa）	Not recorded	IA1 2-[2-[[4-(4-chloranyl-2,5-dimethoxy-phenyl)-5-(2-cyclohexylethyl)-1,3-thiazol-2-yl]carbamoyl]-5,7-dimethyl-indol-1-yl]ethanoic acid × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å
9BKJ Cholecystokinin 1 receptor (CCK1R) Y140A mutant, Gq chimera (mGsqi) complex Deposited 2024-04-29	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 2–428（427 aa）	Mutation：Y140A	NH2 AMINO GROUP × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.59 Å
9BKK Cholecystokinin 1 receptor (CCK1R) sterol 7M mutant, Gq chimera (mGsqi) complex Deposited 2024-04-29	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric	Chain R 2–428（427 aa）	Mutation：F130L, S136A, G141S, I216L, L219F, I223V, M226A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.51 Å

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CCKAR_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–30； UniProt 329–357

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	1hzn
Deposition date deposition_date	2001-01-25
Structure title title	NMR SOLUTION STRUCTURE OF THE THIRD EXTRACELLULAR LOOP OF THE CHOLECYSTOKININ A RECEPTOR
Keywords keywords	HORMONE/GROWTH FACTOR, HORMONE-GROWTH FACTOR complex; HORMONE/GROWTH FACTOR
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	10.59 Å
Radius of gyration Rg (electron density) rg_electron	9.80 Å
Forward intensity I(0) i0	302072.00
Molecular weight molecular_weight	3271.0 kDa
Excluded volume excluded_volume	4140 Å³
Envelope volume envelope_volume	5031 Å³
Hydration-shell volume shell_volume	4989 Å³
Envelope diameter envelope_diameter	31.8 Å
Shell Rg shell_rg	13.83 Å
Envelope Rg envelope_rg	9.94 Å
Shape Rg shape_rg	9.82 Å
Total Rg total_rg	11.27 Å
Total atoms total_atoms	464
Residues n_residues	29
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	36.0 Å
Rg (real space) rg_real	10.59 Å
Rg uncertainty (real space) rg_real_error	0.26 Å
I(0) (real space) i0_real	3.0210e+05
I(0) uncertainty (real space) i0_real_error	3.0360e+03
Rg (reciprocal space) rg_reciprocal	10.59 Å
I(0) (reciprocal space) i0_reciprocal	302100.0000
Solution quality estimate total_estimate	0.8782
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	12.3 Å
Skewness Skewness skewness	0.311
Kurtosis Kurtosis kurtosis	-0.203
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	41400.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.826; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.966

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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	d1hzna_
Class class	j — Peptides
Fold Fold fold	j.82 — Cholecystokinin receptor fragments
Superfamily Superfamily superfamily	j.82.1 — Cholecystokinin receptor fragments
Family Family family	j.82.1.1 — Cholecystokinin receptor fragments

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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	CHOLECYSTOKININ TYPE A RECEPTOR
Molecular weight formula_weight	3254.7 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	464

fit	/app/data/saxs_computation/hz/1hzn/1hzn.fit
pddf	/app/data/pr_computation/hz/1hzn/1hzn.pr.out
profile	/app/data/saxs_computation/hz/1hzn/1hzn.dat

NMR SOLUTION STRUCTURE OF THE THIRD EXTRACELLULAR LOOP OF THE CHOLECYSTOKININ A RECEPTOR

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

CHOLECYSTOKININ TYPE A RECEPTOR

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

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)