SAXSdb — 5v6y

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

Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,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	Insufficient information	Heteromer	Protein 2 其他Polymer 1	ADM × 1 （P35318） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 water × 1	Consistent with protein count
2	Insufficient information	Heteromer	Protein 2 其他Polymer 1	ADM × 1 （P35318） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 water × 1	Consistent with protein count
3	Insufficient information	Heteromer	Protein 2 其他Polymer 1	ADM × 1 （P35318） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1	Consistent with protein count
4	Insufficient information	Heteromer	Protein 2 其他Polymer 1	ADM × 1 （P35318） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1	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	1
Chains and sequence ranges	Author chain A； PDBConstruct 375–462； UniProt 24–111 Author chain B； PDBConstruct 375–462； UniProt 24–111 Author chain C； PDBConstruct 375–462； UniProt 24–111 Author chain D； PDBConstruct 375–462； UniProt 24–111

Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor

Homo sapiens

UniProt P0AEY0

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 2 其他Polymer 1	ADM × 1 （P35318） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 water × 1	Consistent with protein count
2	Insufficient information	Heteromer	Protein 2 其他Polymer 1	ADM × 1 （P35318） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 water × 1	Consistent with protein count
3	Insufficient information	Heteromer	Protein 2 其他Polymer 1	ADM × 1 （P35318） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1	Consistent with protein count
4	Insufficient information	Heteromer	Protein 2 其他Polymer 1	ADM × 1 （P35318） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MALE_ECO57
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–368； UniProt 26–392 Author chain B； PDBConstruct 2–368； UniProt 26–392 Author chain C； PDBConstruct 2–368； UniProt 26–392 Author chain D； PDBConstruct 2–368； UniProt 26–392

Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor

Homo sapiens

UniProt Q16602

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 2 其他Polymer 1	ADM × 1 （P35318） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 water × 1	Consistent with protein count
2	Insufficient information	Heteromer	Protein 2 其他Polymer 1	ADM × 1 （P35318） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 water × 1	Consistent with protein count
3	Insufficient information	Heteromer	Protein 2 其他Polymer 1	ADM × 1 （P35318） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1	Consistent with protein count
4	Insufficient information	Heteromer	Protein 2 其他Polymer 1	ADM × 1 （P35318） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1	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 472–587； UniProt 29–144 Author chain B； PDBConstruct 472–587； UniProt 29–144 Author chain C； PDBConstruct 472–587； UniProt 29–144 Author chain D； PDBConstruct 472–587； UniProt 29–144

ADM

OrganismNot specified

UniProt P35318

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Insufficient information	Heteromer	Protein 2 其他Polymer 1	Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor × 1 （O60894,P0AEY0,Q16602） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 water × 1	Consistent with protein count
2	Insufficient information	Heteromer	Protein 2 其他Polymer 1	Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor × 1 （O60894,P0AEY0,Q16602） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 water × 1	Consistent with protein count
3	Insufficient information	Heteromer	Protein 2 其他Polymer 1	Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor × 1 （O60894,P0AEY0,Q16602） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1	Consistent with protein count
4	Insufficient information	Heteromer	Protein 2 其他Polymer 1	Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor × 1 （O60894,P0AEY0,Q16602） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	ADML_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain E； PDBConstruct 1–16； UniProt 131–146 Author chain F； PDBConstruct 1–16； UniProt 131–146 Author chain G； PDBConstruct 1–16； UniProt 131–146 Author chain H； PDBConstruct 1–16； UniProt 131–146

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	5v6y
Deposition date deposition_date	2017-03-17
Structure title title	Crystal structure of the human CLR:RAMP1 extracellular domain heterodimer with bound high-affinity and altered selectivity adrenomedullin variant
Keywords keywords	class B G protein-coupled receptor, GPCR, calcitonin family peptide, TRANSPORT PROTEIN - MEMBRANE PROTEIN complex; TRANSPORT PROTEIN / MEMBRANE PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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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.

5v6y__assembly_4__model_1

Assembly 4 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

5v6y__assembly_4__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5v6y__assembly_4__model_1 | P(r) · Pending

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

Rg（Guinier）	27.65 Å
Rg (electron density)	26.92 Å
Total Rg	27.76 Å
Atom count	4391
Residues	560
Excluded volume	77863 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5v6y__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`5v6y__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`5v6y__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
4	1	`5v6y__assembly_4__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor
Molecular weight formula_weight	66304.6 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,D
Atom count atom_count	17855

MAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNAAAEFTTACQEANYGALLRELCLTQFQVDMEAVGETLWCDWGRTIRSYRELADCTWHMAEKLGCFWPNAEVDRFFLAVHGRYFRSCPISGRAVGSAGSAGSAEDSIQLGVTRNKIMTAQYECYQKIMQDPIQQAEGVYCNRTWDGWLCWNDVAAGTESMQLCPDYFQDFDPSEKVTKICDQDGNWFRHPASNRTWTNYTQCNVNTHEKVKTALNLFYLHHHHHH

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	ADM
Molecular weight formula_weight	1901.2 kDa
Mutation mutation	S45W, K46L, Q50W, Y52F
Source method src_method	syn
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,F,G,H

DKDNVAPRWLISPWGFX

Entity 3 Entity 3 branched

Description description	alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose
Molecular weight formula_weight	342.3 kDa
Source method src_method	man
Copy count entity_count	4

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	3

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Unit-cell length a length_a	195.496 Å
Unit-cell length b length_b	69.436 Å
Unit-cell length c length_c	200.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	99.43 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	45.114 Å
R factor r_factor	0.2131
R_work r_work	0.2120
R_free r_free	0.2445

Crystal structure of the human CLR:RAMP1 extracellular domain heterodimer with bound high-affinity and altered selectivity adrenomedullin variant

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

Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor

State in the Current Structure

Other States of the Same Protein in the Database

Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor

State in the Current Structure

Other States of the Same Protein in the Database

Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor

State in the Current Structure

Other States of the Same Protein in the Database

ADM

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

5v6y__assembly_4__model_1

5v6y__assembly_4__model_1 | I(q)

5v6y__assembly_4__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 branched

Entity 4 Entity 4 water

7. Citations (1)

Crystal structure of the human CLR:RAMP1 extracellular domain heterodimer with bound high-affinity and altered selectivity adrenomedullin variant

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

Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,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

Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,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

Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,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

ADM

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

5v6y__assembly_4__model_1

5v6y__assembly_4__model_1 | I(q)

5v6y__assembly_4__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 branched

Entity 4 Entity 4 water

7. Citations (1)