SAXSdb — 4rwf

▼

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

Maltose transporter subunit, Receptor activity-modifying protein 2, Calcitonin gene-related peptide type 1 receptor fusion protein

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	Adrenomedullin × 1 （P35318） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 1,2-ETHANEDIOL × 5 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	RAMP2_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 375–458； UniProt 55–138

Maltose transporter subunit, Receptor activity-modifying protein 2, Calcitonin gene-related peptide type 1 receptor fusion protein

Homo sapiens

UniProt P0AEX9

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	Adrenomedullin × 1 （P35318） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 1,2-ETHANEDIOL × 5 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	MALE_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–374； UniProt 26–398

Maltose transporter subunit, Receptor activity-modifying protein 2, Calcitonin gene-related peptide type 1 receptor fusion protein

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	Adrenomedullin × 1 （P35318） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 1,2-ETHANEDIOL × 5 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 472–557； UniProt 31–116

Adrenomedullin

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 transporter subunit, Receptor activity-modifying protein 2, Calcitonin gene-related peptide type 1 receptor fusion protein × 1 （O60895,P0AEX9,Q16602） alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 1,2-ETHANEDIOL × 5 water × 2	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 B； PDBConstruct 1–28； UniProt 119–146

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	4rwf
Deposition date deposition_date	2014-12-03
Structure title title	Crystal structure of the CLR:RAMP2 extracellular domain heterodimer with bound adrenomedullin
Keywords keywords	cell surface receptor, MEMBRANE PROTEIN-HORMONE complex; MEMBRANE PROTEIN/HORMONE
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.

4rwf__assembly_1__model_1

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

Download this curve (.dat)

4rwf__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4rwf__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	27.38 Å
Rg (electron density)	26.46 Å
Total Rg	27.37 Å
Atom count	4583
Residues	573
Excluded volume	81358 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4rwf__assembly_1__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 (5)

Entity 1 Entity 1 polymer

Description description	Maltose transporter subunit, Receptor activity-modifying protein 2, Calcitonin gene-related peptide type 1 receptor fusion protein
Molecular weight formula_weight	66308.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	5009

MAKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEALKDAQTNAAAEFGGTVKNYETAVQFCWNHYKDQMDPIEKDWCDWAMISRPYSTLRDCLEHFAERFDLGFPNPLAERIIFETHQIHFANCSLVQPTFSDGSAGSAGSAEDSIQLGVTRNKIMTAQYECYQKIMQDPIQQAEGVYCNRTWDGWLCWNDVAAGTESMQLCPDYFQDFDPSEKVTKICDQDGNWFRHPASNRTWTNYTQCNVNTHEKVKTALNLFYLHHHHHH

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	Adrenomedullin
Molecular weight formula_weight	3252.7 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

KLAHQIYQFTDKDKDNVAPRSKISPQGYX

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	1

Entity 4 Entity 4 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	394

▼

6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	4rwfA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily	10 — Periplasmic binding protein-like II

▶

Unit-cell length a length_a	71.454 Å
Unit-cell length b length_b	84.283 Å
Unit-cell length c length_c	115.764 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	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	1.760 Å
Low-resolution limit resolution_low	50.000 Å
R factor r_factor	0.1590
R_work r_work	0.1569
R_free r_free	0.2003

Crystal structure of the CLR:RAMP2 extracellular domain heterodimer with bound adrenomedullin

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

Maltose transporter subunit, Receptor activity-modifying protein 2, Calcitonin gene-related peptide type 1 receptor fusion protein

State in the Current Structure

Other States of the Same Protein in the Database

Maltose transporter subunit, Receptor activity-modifying protein 2, Calcitonin gene-related peptide type 1 receptor fusion protein

State in the Current Structure

Other States of the Same Protein in the Database

Maltose transporter subunit, Receptor activity-modifying protein 2, Calcitonin gene-related peptide type 1 receptor fusion protein

State in the Current Structure

Other States of the Same Protein in the Database

Adrenomedullin

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

4rwf__assembly_1__model_1

4rwf__assembly_1__model_1 | I(q)

4rwf__assembly_1__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 (5)

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 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

7. Citations (1)

Crystal structure of the CLR:RAMP2 extracellular domain heterodimer with bound adrenomedullin

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

Maltose transporter subunit, Receptor activity-modifying protein 2, Calcitonin gene-related peptide type 1 receptor fusion protein

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 transporter subunit, Receptor activity-modifying protein 2, Calcitonin gene-related peptide type 1 receptor fusion protein

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 transporter subunit, Receptor activity-modifying protein 2, Calcitonin gene-related peptide type 1 receptor fusion protein

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Adrenomedullin

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

4rwf__assembly_1__model_1

4rwf__assembly_1__model_1 | I(q)

4rwf__assembly_1__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 (5)

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 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

7. Citations (1)