5hk5

Structure of the Grem2-GDF5 Inhibitory Complex

Method: X-RAY DIFFRACTION Dmax: 133.6 Å Quality: GOOD

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

Gremlin-2

Mus musculus

UniProt O88273

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 22–168 Chain F; UniProt 22–168 Not recorded Growth/differentiation factor 5 × 2 (P43026) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;HEPES, ammonium chloride, ethylammonium nitrate Resolution 2.90 Å R-free 0.282
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 22–168 Chain F; UniProt 22–168 Not recorded Growth/differentiation factor 5 × 2 (P43026) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;HEPES, ammonium chloride, ethylammonium nitrate Resolution 2.90 Å R-free 0.282
3 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 22–168 Chain H; UniProt 22–168 Not recorded Growth/differentiation factor 5 × 2 (P43026) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;HEPES, ammonium chloride, ethylammonium nitrate Resolution 2.90 Å R-free 0.282
4 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 22–168 Chain H; UniProt 22–168 Not recorded Growth/differentiation factor 5 × 2 (P43026) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;HEPES, ammonium chloride, ethylammonium nitrate Resolution 2.90 Å R-free 0.282

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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GREM2_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain E; PDBConstruct 1–147; UniProt 22–168 Author chain F; PDBConstruct 1–147; UniProt 22–168 Author chain G; PDBConstruct 1–147; UniProt 22–168 Author chain H; PDBConstruct 1–147; UniProt 22–168

Growth/differentiation factor 5

Homo sapiens

UniProt P43026

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 382–501 Chain C; UniProt 382–501 Not recorded Gremlin-2 × 2 (O88273) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;HEPES, ammonium chloride, ethylammonium nitrate Resolution 2.90 Å R-free 0.282
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 382–501 Chain C; UniProt 382–501 Not recorded Gremlin-2 × 2 (O88273) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;HEPES, ammonium chloride, ethylammonium nitrate Resolution 2.90 Å R-free 0.282
3 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 382–501 Chain D; UniProt 382–501 Not recorded Gremlin-2 × 2 (O88273) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;HEPES, ammonium chloride, ethylammonium nitrate Resolution 2.90 Å R-free 0.282
4 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 382–501 Chain D; UniProt 382–501 Not recorded Gremlin-2 × 2 (O88273) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;HEPES, ammonium chloride, ethylammonium nitrate Resolution 2.90 Å R-free 0.282

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.

14 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GDF5_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–120; UniProt 382–501 Author chain B; PDBConstruct 1–120; UniProt 382–501 Author chain C; PDBConstruct 1–120; UniProt 382–501 Author chain D; PDBConstruct 1–120; UniProt 382–501

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 5hk5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5hk5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5hk5
Deposition date deposition_date2016-01-13
Structure title titleStructure of the Grem2-GDF5 Inhibitory Complex
Keywords keywordsDAN-family, Bone Morphogenetic Proteins, CYTOKINE; CYTOKINE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.70
Radius of gyration Rg (electron density) rg_electron36.82
Forward intensity I(0) i0183191000.00
Molecular weight molecular_weight106300.0 kDa
Excluded volume excluded_volume132160 ų
Envelope volume envelope_volume188990 ų
Hydration-shell volume shell_volume44616 ų
Envelope diameter envelope_diameter139.2
Shell Rg shell_rg40.61
Envelope Rg envelope_rg37.26
Shape Rg shape_rg36.87
Total Rg total_rg36.92
Total atoms total_atoms7425
Residues n_residues925
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 dmax133.6
Rg (real space) rg_real36.87
Rg uncertainty (real space) rg_real_error1.73
I(0) (real space) i0_real1.8320e+08
I(0) uncertainty (real space) i0_real_error3.2660e+06
Rg (reciprocal space) rg_reciprocal36.77
I(0) (reciprocal space) i0_reciprocal183200000.0000
Solution quality estimate total_estimate0.8450
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.5
Skewness Skewness skewness0.483
Kurtosis Kurtosis kurtosis-0.023
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22810000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.734; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.836; Smooth: 0.944

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 11 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd5hk5a_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.0 — automated matches
Domain ID domain_idd5hk5b_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.0 — automated matches
Domain ID domain_idd5hk5c_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.0 — automated matches
Domain ID domain_idd5hk5d_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.0 — automated matches

CATH v4.4 (7 domains)

Domain ID domain_id5hk5A00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id5hk5B00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id5hk5C00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id5hk5D00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id5hk5E00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id5hk5F00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id5hk5G00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines

8. Citations (1)

9. Files and Curves (10)