6z3g

Repulsive Guidance Molecule A (RGMA) in complex with Growth Differentiation Factor 5 (GDF5)

Method: X-RAY DIFFRACTION Dmax: 65.2 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 Repulsive guidance molecule A × 2 (Q96B86) CIT CITRIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.5, 24% v/v polyethylene glycol (PEG) 400. Resolution 2.78 Å R-free 0.288

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

Repulsive guidance molecule A

Homo sapiens

UniProt Q96B86

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 54–139 Not recorded Growth/differentiation factor 5 × 2 (P43026) CIT CITRIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.2 M ammonium acetate, 0.1 M sodium citrate tribasic dihydrate pH 5.5, 24% v/v polyethylene glycol (PEG) 400. Resolution 2.78 Å R-free 0.288

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 RGMA_HUMAN
Isoform Q96B86-4
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 12–97; UniProt 54–139

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 6z3g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6z3g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6z3g
Deposition date deposition_date2020-05-20
Structure title titleRepulsive Guidance Molecule A (RGMA) 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., 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_guinier20.88
Radius of gyration Rg (electron density) rg_electron20.07
Forward intensity I(0) i06839560.00
Molecular weight molecular_weight18353.0 kDa
Excluded volume excluded_volume22489 ų
Envelope volume envelope_volume31147 ų
Hydration-shell volume shell_volume13546 ų
Envelope diameter envelope_diameter65.5
Shell Rg shell_rg25.62
Envelope Rg envelope_rg19.72
Shape Rg shape_rg20.04
Total Rg total_rg20.99
Total atoms total_atoms1278
Residues n_residues162
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 dmax65.2
Rg (real space) rg_real20.85
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real6.8400e+06
I(0) uncertainty (real space) i0_real_error9.4390e+04
Rg (reciprocal space) rg_reciprocal20.86
I(0) (reciprocal space) i0_reciprocal6840000.0000
Solution quality estimate total_estimate0.9052
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.1
Skewness Skewness skewness0.095
Kurtosis Kurtosis kurtosis-0.782
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha573900.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.946; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.944; Smooth: 0.981

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_idd6z3ga_
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)