SAXSdb — 1gea

▼

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

PITUITARY ADENYLATE CYCLASE ACTIVATING POLYPEPTIDE

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 132–152	Fragment：N-TERMINAL DOMAIN(RESIDUE 132-152) Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	SOLUTION NMR NMR measurement conditions：pH 6.3；298 K；Ionic strength (raw mmCIF value) 0.41；Pressure ambient NMR sample composition：1.7mM PACAP21; 40mM PACAP receptor; 80mM phosphate buffer (pH 6.3) \| 90% H2O/10% D2O NMR sample composition：1.7mM PACAP21; 40mM PACAP receptor; 80mM phosphate buffer (pH 6.3) \| 99.8% 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 1GEA	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
2D2P The solution structure of micelle-bound peptide Deposited 2005-09-14	Different construct Different experimental conditions	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 132–169（38 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 20mM potassium phosphate；Pressure ambient NMR sample composition 0.5mM PACAP38 U-15N,13C; 20mM potassium phosphate buffer; 200mM DPC; 93% H2O, 5% D2O, 2% Glycerol-1,1,2,3,3-d5 \| 93% H2O, 5% D2O, 2% Glycerol-1,1,2,3,3-d5	Resolution not provided
2JOD Pac1-Rshort N-terminal EC domain Pacap(6-38) complex Deposited 2007-03-07	Different construct Different mutation/modification Different oligomeric state Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 137–169（33 aa） Fragment：sequence database residues, 137-169	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 100；Pressure ambient NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] pac1-R N-terminal EC domain, 0.5 mM PACAP (6-38), 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
6LPB Cryo-EM structure of the human PAC1 receptor coupled to an engineered heterotrimeric G protein Deposited 2020-01-09	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 P 132–169（38 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.90 Å
6M1I CryoEM structure of human PAC1 receptor in complex with PACAP38 Deposited 2020-02-26	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 B 132–169（38 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.50 Å
6P9Y PAC1 GPCR Receptor complex Deposited 2019-06-10	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 132–169（38 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.01 Å
6VN7 Cryo-EM structure of an activated VIP1 receptor-G protein complex Deposited 2020-01-29	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 L 132–158（27 aa）	Not recorded	CLR CHOLESTEROL × 6 PLM PALMITIC ACID × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å
7VQX Cryo-EM structure of human vasoactive intestinal polypeptide receptor 2 (VIP2R) in complex with PACAP27 and Gs Deposited 2021-10-21	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 L 132–158（27 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.74 Å
7WBJ Cryo-EM structure of N-terminal modified human vasoactive intestinal polypeptide receptor 2 (VIP2R) in complex with PACAP27 and Gs Deposited 2021-12-16	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 L 132–158（27 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.42 Å
8E3X Cryo-EM structure of the PAC1R-PACAP27-Gs complex Deposited 2022-08-17	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 P 132–158（27 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.30 Å
8E3Y Cryo-EM structure of the VPAC1R-PACAP27-Gs complex Deposited 2022-08-17	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 P 132–158（27 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.30 Å
9P94 Cryo-EM structure of the PAC1sR-PACAP27-Gs complex Deposited 2025-06-24	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 P 132–158（27 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.00 Å

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

View Construct and Data Evidence

UniProt name	PACA_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–21； UniProt 132–152

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1gea
Deposition date deposition_date	2000-10-20
Structure title title	RECEPTOR-BOUND CONFORMATION OF PACAP21
Keywords keywords	BETA COIL, CONSECUTIVE BETA TURNS, TYPE-II BETA TURN, TYPE-I BETA TURN, HELIX, NEUROPEPTIDE; NEUROPEPTIDE
Experimental Method method	SOLUTION NMR

▼

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

Radius of gyration Rg (Guinier) rg_guinier	8.98 Å
Radius of gyration Rg (electron density) rg_electron	9.17 Å
Forward intensity I(0) i0	61838100.00
Molecular weight molecular_weight	63023.0 kDa
Excluded volume excluded_volume	78040 Å³
Envelope volume envelope_volume	9249 Å³
Hydration-shell volume shell_volume	7542 Å³
Envelope diameter envelope_diameter	36.9 Å
Shell Rg shell_rg	16.14 Å
Envelope Rg envelope_rg	11.45 Å
Shape Rg shape_rg	9.14 Å
Total Rg total_rg	9.54 Å
Total atoms total_atoms	8875
Residues n_residues	500
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

▼

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

Maximum dimension Dmax dmax	35.2 Å
Rg (real space) rg_real	9.15 Å
Rg uncertainty (real space) rg_real_error	0.49 Å
I(0) (real space) i0_real	6.1840e+07
I(0) uncertainty (real space) i0_real_error	6.4930e+05
Rg (reciprocal space) rg_reciprocal	9.15 Å
I(0) (reciprocal space) i0_reciprocal	61840000.0000
Solution quality estimate total_estimate	0.5571
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	8.0 Å
Skewness Skewness skewness	0.659
Kurtosis Kurtosis kurtosis	-0.032
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	4789.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.476; Stabil: 0.999; Sysdev: 0.256; Positv: 1.000; Valcen: 0.117; Smooth: 0.926

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▼

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1geaa_
Class class	j — Peptides
Fold Fold fold	j.81 — Pituitary adenylate cyclase activating polypeptide, pacap21
Superfamily Superfamily superfamily	j.81.1 — Pituitary adenylate cyclase activating polypeptide, pacap21
Family Family family	j.81.1.1 — Pituitary adenylate cyclase activating polypeptide, pacap21

▶

8. Citations (1)

▶

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	PITUITARY ADENYLATE CYCLASE ACTIVATING POLYPEPTIDE
Molecular weight formula_weight	2522.9 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	8875

fit	/app/data/saxs_computation/ge/1gea/1gea.fit
pddf	/app/data/pr_computation/ge/1gea/1gea.pr.out
profile	/app/data/saxs_computation/ge/1gea/1gea.dat

RECEPTOR-BOUND CONFORMATION OF PACAP21

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

PITUITARY ADENYLATE CYCLASE ACTIVATING POLYPEPTIDE

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)