SAXSdb — 3n7p

▼

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

Calcitonin gene-related peptide type 1 receptor

Homo sapiens

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Receptor activity-modifying protein 1 × 1 （O60894） SULFATE ION × 6 water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Receptor activity-modifying protein 1 × 1 （O60894） SULFATE ION × 6 water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	Receptor activity-modifying protein 1 × 1 （O60894） water × 2	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	Receptor activity-modifying protein 1 × 1 （O60894） SULFATE ION × 4 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CALRL_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–115； UniProt 23–133 Author chain B； PDBConstruct 5–115； UniProt 23–133 Author chain C； PDBConstruct 5–115； UniProt 23–133 Author chain J； PDBConstruct 5–115； UniProt 23–133

Receptor activity-modifying protein 1

Homo sapiens

UniProt O60894

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 2	Calcitonin gene-related peptide type 1 receptor × 1 （Q16602） SULFATE ION × 6 water × 2	Consistent with protein count
2	Protein heterocomplex	Heteromer	Protein 2	Calcitonin gene-related peptide type 1 receptor × 1 （Q16602） SULFATE ION × 6 water × 2	Consistent with protein count
3	Protein heterocomplex	Heteromer	Protein 2	Calcitonin gene-related peptide type 1 receptor × 1 （Q16602） water × 2	Consistent with protein count
4	Protein heterocomplex	Heteromer	Protein 2	Calcitonin gene-related peptide type 1 receptor × 1 （Q16602） SULFATE ION × 4 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RAMP1_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain D； PDBConstruct 5–96； UniProt 26–117 Author chain E； PDBConstruct 5–96； UniProt 26–117 Author chain F； PDBConstruct 5–96； UniProt 26–117 Author chain R； PDBConstruct 5–96； UniProt 26–117

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	3n7p
Deposition date deposition_date	2010-05-27
Structure title title	Crystal structure of the ectodomain complex of the CGRP receptor, a Class-B GPCR, reveals the site of drug antagonism
Keywords keywords	GPCR, class B GPCR, antagonist, olcegepant, telcagepant, migraine, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method method	X-RAY DIFFRACTION

▼

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

3n7p__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3n7p__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3n7p__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	22.26 Å
Rg (electron density)	21.66 Å
Total Rg	22.33 Å
Atom count	1506
Residues	188
Excluded volume	25976 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3n7p__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`3n7p__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`3n7p__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`3n7p__assembly_4__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Calcitonin gene-related peptide type 1 receptor
Molecular weight formula_weight	13572.4 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,J
Atom count atom_count	5529

GSHMELEESPEDSIQLGVTRNKIMTAQYECYQKIMQDPIQQAEGVYCNRTWDGWLCWNDVAAGTESMQLCPDYFQDFDPSEKVTKICDQDGNWFRHPASNRTWTNYTQCNVNTHE

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Receptor activity-modifying protein 1
Molecular weight formula_weight	11002.5 kDa
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,E,F,R

GSHMACQEANYGALLRELCLTQFQVDMEAVGETLWCDWGRTIRSYRELADCTWHMAEKLGCFWPNAEVDRFFLAVHGRYFRSCPISGRAVRDPPGS

Source Source

Source organism organism	Homo sapiens
Common name common_name	human
NCBI taxonomy ID ncbi_taxonomy_id	9606
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	16

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	53

▼

6. Fold Classification (SCOP + CATH) 7 domains

CATH v4.4 (7 domains)

Domain ID domain_id	3n7pA00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	1240 — Hormone receptor fold
Homologous superfamily homologous superfamily	10 — GPCR, family 2, extracellular hormone receptor domain

Domain ID domain_id	3n7pB00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	1240 — Hormone receptor fold
Homologous superfamily homologous superfamily	10 — GPCR, family 2, extracellular hormone receptor domain

Domain ID domain_id	3n7pD00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily	510 — Receptor activity modifying family

Domain ID domain_id	3n7pE00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily	510 — Receptor activity modifying family

Domain ID domain_id	3n7pF00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily	510 — Receptor activity modifying family

Domain ID domain_id	3n7pJ00
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	1240 — Hormone receptor fold
Homologous superfamily homologous superfamily	10 — GPCR, family 2, extracellular hormone receptor domain

Domain ID domain_id	3n7pR00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily	510 — Receptor activity modifying family

▶

Unit-cell length a length_a	118.000 Å
Unit-cell length b length_b	118.000 Å
Unit-cell length c length_c	225.400 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	24

Space group space_group	P 32 2 1
Space-group number int_tables_number	154
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	27.120 Å
R factor r_factor	0.2151
R_work r_work	0.2138
R_free r_free	0.2408

Crystal structure of the ectodomain complex of the CGRP receptor, a Class-B GPCR, reveals the site of drug antagonism

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

Calcitonin gene-related peptide type 1 receptor

State in the Current Structure

Other States of the Same Protein in the Database

Receptor activity-modifying protein 1

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

3n7p__assembly_1__model_1

3n7p__assembly_1__model_1 | I(q)

3n7p__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 7 domains

CATH v4.4 (7 domains)

7. Citations (1)

Crystal structure of the ectodomain complex of the CGRP receptor, a Class-B GPCR, reveals the site of drug antagonism

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

Calcitonin gene-related peptide type 1 receptor

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Receptor activity-modifying protein 1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

3n7p__assembly_1__model_1

3n7p__assembly_1__model_1 | I(q)

3n7p__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 7 domains

CATH v4.4 (7 domains)

7. Citations (1)