5nhr

CRYSTAL STRUCTURE OF THE Activin receptor type-2B LIGAND BINDING DOMAIN IN COMPLEX WITH BIMAGRUMAB FV, CUBIC CRYSTAL FORM

Method: X-RAY DIFFRACTION Dmax: 116.6 Å Quality: GOOD

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

Activin receptor type-2B

Homo sapiens

UniProt Q13705

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 24–117 Fragment:VL, UNP residues 24-117 Bimagrumab Fv Light-Chain × 1 Bimagrumab Fv heavy-chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 4.6;293 K;1.4M AMMONIUM SULFATE, 0.1M SODIUM CITRATE Resolution 3.35 Å R-free 0.229
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 24–117 Fragment:VL, UNP residues 24-117 Bimagrumab Fv Light-Chain × 1 Bimagrumab Fv heavy-chain × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 4.6;293 K;1.4M AMMONIUM SULFATE, 0.1M SODIUM CITRATE Resolution 3.35 Å R-free 0.229

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 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AVR2B_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 6–99; UniProt 24–117 Author chain D; PDBConstruct 6–99; UniProt 24–117

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.

SAXS scattering curve SAXS Profile

SAXS profile for 5nhr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5nhr
Deposition date deposition_date2017-03-22
Structure title titleCRYSTAL STRUCTURE OF THE Activin receptor type-2B LIGAND BINDING DOMAIN IN COMPLEX WITH BIMAGRUMAB FV, CUBIC CRYSTAL FORM
Keywords keywordsthree-finger toxin fold, antibody Fv fragment, immune system; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.39
Radius of gyration Rg (electron density) rg_electron34.00
Forward intensity I(0) i084492500.00
Molecular weight molecular_weight70030.0 kDa
Excluded volume excluded_volume85972 ų
Envelope volume envelope_volume115250 ų
Hydration-shell volume shell_volume29178 ų
Envelope diameter envelope_diameter115.9
Shell Rg shell_rg39.33
Envelope Rg envelope_rg33.52
Shape Rg shape_rg33.98
Total Rg total_rg34.45
Total atoms total_atoms4918
Residues n_residues636
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 dmax116.6
Rg (real space) rg_real34.65
Rg uncertainty (real space) rg_real_error1.33
I(0) (real space) i0_real8.4490e+07
I(0) uncertainty (real space) i0_real_error1.5010e+06
Rg (reciprocal space) rg_reciprocal34.49
I(0) (reciprocal space) i0_reciprocal84480000.0000
Solution quality estimate total_estimate0.8215
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.9
Skewness Skewness skewness0.419
Kurtosis Kurtosis kurtosis-0.665
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7430000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.711; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.693; Smooth: 0.849

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id5nhrB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id5nhrC00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59
Domain ID domain_id5nhrD00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59
Domain ID domain_id5nhrL00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)