6z3l

Repulsive Guidance Molecule C (RGMC, Hemojuvelin, HJV, HFE2) in complex with Growth Differentiation Factor 5 (GDF5)

Method: X-RAY DIFFRACTION Dmax: 64.2 Å Quality: EXCELLENT

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

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 387–501 Not recorded Hemojuvelin × 2 (Q6ZVN8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;1 M LiCl, 0.1 M citric acid pH 4.0, 8% gamma-butyrolactone. Resolution 2.51 Å R-free 0.267

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 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GDF5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–117; UniProt 387–501

Hemojuvelin

Homo sapiens

UniProt Q6ZVN8

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 B; UniProt 36–145 Not recorded Growth/differentiation factor 5 × 2 (P43026) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;1 M LiCl, 0.1 M citric acid pH 4.0, 8% gamma-butyrolactone. Resolution 2.51 Å R-free 0.267

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 RGMC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–113; UniProt 36–145

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 6z3l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6z3l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6z3l
Deposition date deposition_date2020-05-20
Structure title titleRepulsive Guidance Molecule C (RGMC, Hemojuvelin, HJV, HFE2) in complex with Growth Differentiation Factor 5 (GDF5)
Keywords keywords;Repulsive Guidance Molecule, RGM, Bone Morphogenetic Protein, BMP, Growth Differentiation Factor 5, GDF5, Neogenin, axon guidance, TGFbeta signalling, brain development, iron metabolism, Hemojuvelin, HJV, HFE2, hemochromatosis type 2 protein, juvenile hemochromatosis., SIGNALING PROTEIN ;; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.71
Radius of gyration Rg (electron density) rg_electron19.85
Forward intensity I(0) i06176240.00
Molecular weight molecular_weight17531.0 kDa
Excluded volume excluded_volume21520 ų
Envelope volume envelope_volume29450 ų
Hydration-shell volume shell_volume13001 ų
Envelope diameter envelope_diameter63.8
Shell Rg shell_rg25.33
Envelope Rg envelope_rg19.47
Shape Rg shape_rg19.83
Total Rg total_rg20.74
Total atoms total_atoms1220
Residues n_residues157
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 dmax64.2
Rg (real space) rg_real20.68
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real6.1760e+06
I(0) uncertainty (real space) i0_real_error8.0520e+04
Rg (reciprocal space) rg_reciprocal20.69
I(0) (reciprocal space) i0_reciprocal6176000.0000
Solution quality estimate total_estimate0.9067
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.6
Skewness Skewness skewness0.091
Kurtosis Kurtosis kurtosis-0.813
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha500000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.950; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.936; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6z3la_
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

8. Citations (1)

9. Files and Curves (10)