5v6y

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

Method: X-RAY DIFFRACTION Dmax: 153.1 Å Quality: GOOD

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

UniProt O60894

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 24–111 Not recorded ADM × 1 (P35318) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;15% PEG3350, 0.1 M Sodium Malonate pH 6.0, 50 mM Potassium/Sodium tartrate, 1% Cadaverine Resolution 2.80 Å R-free 0.244
2 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 24–111 Not recorded ADM × 1 (P35318) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;15% PEG3350, 0.1 M Sodium Malonate pH 6.0, 50 mM Potassium/Sodium tartrate, 1% Cadaverine Resolution 2.80 Å R-free 0.244
3 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 24–111 Not recorded ADM × 1 (P35318) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;15% PEG3350, 0.1 M Sodium Malonate pH 6.0, 50 mM Potassium/Sodium tartrate, 1% Cadaverine Resolution 2.80 Å R-free 0.244
4 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 24–111 Not recorded ADM × 1 (P35318) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;15% PEG3350, 0.1 M Sodium Malonate pH 6.0, 50 mM Potassium/Sodium tartrate, 1% Cadaverine Resolution 2.80 Å R-free 0.244

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.

25 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 26–392 Not recorded ADM × 1 (P35318) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;15% PEG3350, 0.1 M Sodium Malonate pH 6.0, 50 mM Potassium/Sodium tartrate, 1% Cadaverine Resolution 2.80 Å R-free 0.244
2 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 26–392 Not recorded ADM × 1 (P35318) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;15% PEG3350, 0.1 M Sodium Malonate pH 6.0, 50 mM Potassium/Sodium tartrate, 1% Cadaverine Resolution 2.80 Å R-free 0.244
3 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 26–392 Not recorded ADM × 1 (P35318) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;15% PEG3350, 0.1 M Sodium Malonate pH 6.0, 50 mM Potassium/Sodium tartrate, 1% Cadaverine Resolution 2.80 Å R-free 0.244
4 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 26–392 Not recorded ADM × 1 (P35318) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;15% PEG3350, 0.1 M Sodium Malonate pH 6.0, 50 mM Potassium/Sodium tartrate, 1% Cadaverine Resolution 2.80 Å R-free 0.244

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.

109 other PDB entries and 145 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 29–144 Not recorded ADM × 1 (P35318) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;15% PEG3350, 0.1 M Sodium Malonate pH 6.0, 50 mM Potassium/Sodium tartrate, 1% Cadaverine Resolution 2.80 Å R-free 0.244
2 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 29–144 Not recorded ADM × 1 (P35318) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;15% PEG3350, 0.1 M Sodium Malonate pH 6.0, 50 mM Potassium/Sodium tartrate, 1% Cadaverine Resolution 2.80 Å R-free 0.244
3 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 29–144 Not recorded ADM × 1 (P35318) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;15% PEG3350, 0.1 M Sodium Malonate pH 6.0, 50 mM Potassium/Sodium tartrate, 1% Cadaverine Resolution 2.80 Å R-free 0.244
4 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 29–144 Not recorded ADM × 1 (P35318) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;15% PEG3350, 0.1 M Sodium Malonate pH 6.0, 50 mM Potassium/Sodium tartrate, 1% Cadaverine Resolution 2.80 Å R-free 0.244

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.

24 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 131–146 Mutation:S45W, K46L, Q50W, Y52F Non-standard monomer:Yes (specific site not provided by mmCIF) Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor × 1 (P0AEY0,O60894,Q16602) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;15% PEG3350, 0.1 M Sodium Malonate pH 6.0, 50 mM Potassium/Sodium tartrate, 1% Cadaverine Resolution 2.80 Å R-free 0.244
2 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 131–146 Mutation:S45W, K46L, Q50W, Y52F Non-standard monomer:Yes (specific site not provided by mmCIF) Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor × 1 (P0AEY0,O60894,Q16602) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;15% PEG3350, 0.1 M Sodium Malonate pH 6.0, 50 mM Potassium/Sodium tartrate, 1% Cadaverine Resolution 2.80 Å R-free 0.244
3 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 131–146 Mutation:S45W, K46L, Q50W, Y52F Non-standard monomer:Yes (specific site not provided by mmCIF) Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor × 1 (P0AEY0,O60894,Q16602) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;15% PEG3350, 0.1 M Sodium Malonate pH 6.0, 50 mM Potassium/Sodium tartrate, 1% Cadaverine Resolution 2.80 Å R-free 0.244
4 Insufficient information Heteromer Protein × 2 其他Polymer 1 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 131–146 Mutation:S45W, K46L, Q50W, Y52F Non-standard monomer:Yes (specific site not provided by mmCIF) Maltose-binding periplasmic protein,Receptor activity-modifying protein 1,Calcitonin gene-related peptide type 1 receptor × 1 (P0AEY0,O60894,Q16602) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;15% PEG3350, 0.1 M Sodium Malonate pH 6.0, 50 mM Potassium/Sodium tartrate, 1% Cadaverine Resolution 2.80 Å R-free 0.244

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

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.

SAXS scattering curve SAXS Profile

SAXS profile for 5v6y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5v6y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5v6y
Deposition date deposition_date2017-03-17
Structure title titleCrystal structure of the human CLR:RAMP1 extracellular domain heterodimer with bound high-affinity and altered selectivity adrenomedullin variant
Keywords keywordsclass B G protein-coupled receptor, GPCR, calcitonin family peptide, TRANSPORT PROTEIN - MEMBRANE PROTEIN complex; TRANSPORT PROTEIN / MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier48.54
Radius of gyration Rg (electron density) rg_electron48.32
Forward intensity I(0) i0917563000.00
Molecular weight molecular_weight252910.0 kDa
Excluded volume excluded_volume316540 ų
Envelope volume envelope_volume444460 ų
Hydration-shell volume shell_volume77472 ų
Envelope diameter envelope_diameter161.1
Shell Rg shell_rg51.78
Envelope Rg envelope_rg46.90
Shape Rg shape_rg48.29
Total Rg total_rg48.56
Total atoms total_atoms17838
Residues n_residues2253
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax153.1
Rg (real space) rg_real48.57
Rg uncertainty (real space) rg_real_error1.17
I(0) (real space) i0_real9.1760e+08
I(0) uncertainty (real space) i0_real_error1.6630e+07
Rg (reciprocal space) rg_reciprocal48.54
I(0) (reciprocal space) i0_reciprocal917500000.0000
Solution quality estimate total_estimate0.8534
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.4
Skewness Skewness skewness0.306
Kurtosis Kurtosis kurtosis-0.498
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha65150000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.958; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.218

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)