7mrz

Structure of GDF11 bound to fused ActRIIB-ECD and Alk4-ECD with Anti-ActRIIB Fab fragment

Method: X-RAY DIFFRACTION Dmax: 129.1 Å Quality: GOOD

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

Growth/differentiation factor 11

Homo sapiens

UniProt O95390

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 299–407 Not recorded Activin receptor type-2B,Activin receptor type-1B × 2 (Q13705,P36896) Fab Heavy Chain × 2 Fab Light Chain × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;0.1M HEPES, 0.9M ammonium sulfate, 0.9 M KCl Resolution 3.00 Å R-free 0.327

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GDF11_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–109; UniProt 299–407

Activin receptor type-2B,Activin receptor type-1B

Homo sapiens

UniProt P36896

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 24–126 Fragment:Extracellular domains of both proteins in the fused construct Growth/differentiation factor 11 × 2 (O95390) Fab Heavy Chain × 2 Fab Light Chain × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;0.1M HEPES, 0.9M ammonium sulfate, 0.9 M KCl Resolution 3.00 Å R-free 0.327

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACV1B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 134–236; UniProt 24–126

Activin receptor type-2B,Activin receptor type-1B

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 Insufficient information Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 19–134 Fragment:Extracellular domains of both proteins in the fused construct Growth/differentiation factor 11 × 2 (O95390) Fab Heavy Chain × 2 Fab Light Chain × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;0.1M HEPES, 0.9M ammonium sulfate, 0.9 M KCl Resolution 3.00 Å R-free 0.327

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 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AVR2B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–116; UniProt 19–134

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 7mrz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7mrz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7mrz
Deposition date deposition_date2021-05-10
Structure title titleStructure of GDF11 bound to fused ActRIIB-ECD and Alk4-ECD with Anti-ActRIIB Fab fragment
Keywords keywords;Growth factor, type I receptor, Transforming growth factor beta, type II receptor, ternary complex, GDF11, SIGNALING PROTEIN, SIGNALING PROTEIN-IMMUNE SYSTEM complex ;; SIGNALING PROTEIN/IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.00
Radius of gyration Rg (electron density) rg_electron37.25
Forward intensity I(0) i0107207000.00
Molecular weight molecular_weight79815.0 kDa
Excluded volume excluded_volume98471 ų
Envelope volume envelope_volume137040 ų
Hydration-shell volume shell_volume34139 ų
Envelope diameter envelope_diameter138.9
Shell Rg shell_rg38.28
Envelope Rg envelope_rg37.74
Shape Rg shape_rg37.17
Total Rg total_rg37.59
Total atoms total_atoms10892
Residues n_residues722
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 dmax129.1
Rg (real space) rg_real37.59
Rg uncertainty (real space) rg_real_error1.48
I(0) (real space) i0_real1.0720e+08
I(0) uncertainty (real space) i0_real_error1.9040e+06
Rg (reciprocal space) rg_reciprocal37.22
I(0) (reciprocal space) i0_reciprocal107200000.0000
Solution quality estimate total_estimate0.7745
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.0
Skewness Skewness skewness0.661
Kurtosis Kurtosis kurtosis-0.136
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7682000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.687; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.547; Smooth: 0.457

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 5 domains

CATH v4.4 (5 domains)

Domain ID domain_id7mrzC01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59
Domain ID domain_id7mrzX01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7mrzX02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7mrzY01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7mrzY02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)