6z3m

Repulsive Guidance Molecule B (RGMB) in complex with Growth Differentiation Factor 5 (GDF5) and Neogenin 1 (NEO1).

Method: X-RAY DIFFRACTION Dmax: 230.1 Å Quality: GOOD

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 387–501 Chain B; UniProt 387–501 Not recorded RGM domain family member B × 6 (Q6NW40) Neogenin × 2 (P97798) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.1 M NaCl, 20 mM MES pH 6.7, 6.6% w/v PEG 4000 Resolution 5.50 Å R-free 0.428
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain G; UniProt 387–501 Chain H; UniProt 387–501 Not recorded RGM domain family member B × 6 (Q6NW40) Neogenin × 2 (P97798) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.1 M NaCl, 20 mM MES pH 6.7, 6.6% w/v PEG 4000 Resolution 5.50 Å R-free 0.428
3 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain M; UniProt 387–501 Chain N; UniProt 387–501 Not recorded RGM domain family member B × 6 (Q6NW40) Neogenin × 2 (P97798) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.1 M NaCl, 20 mM MES pH 6.7, 6.6% w/v PEG 4000 Resolution 5.50 Å R-free 0.428

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 20 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 Author chain B; PDBConstruct 3–117; UniProt 387–501 Author chain G; PDBConstruct 3–117; UniProt 387–501 Author chain H; PDBConstruct 3–117; UniProt 387–501 Author chain M; PDBConstruct 3–117; UniProt 387–501 Author chain N; PDBConstruct 3–117; UniProt 387–501

RGM domain family member B

Homo sapiens

UniProt Q6NW40

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain C; UniProt 53–412 Chain D; UniProt 53–412 Chain S; UniProt 53–412 Chain T; UniProt 53–412 Chain c; UniProt 53–412 Chain d; UniProt 53–412 Not recorded Growth/differentiation factor 5 × 2 (P43026) Neogenin × 2 (P97798) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.1 M NaCl, 20 mM MES pH 6.7, 6.6% w/v PEG 4000 Resolution 5.50 Å R-free 0.428
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain I; UniProt 53–412 Chain J; UniProt 53–412 Chain U; UniProt 53–412 Chain V; UniProt 53–412 Chain i; UniProt 53–412 Chain j; UniProt 53–412 Not recorded Growth/differentiation factor 5 × 2 (P43026) Neogenin × 2 (P97798) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.1 M NaCl, 20 mM MES pH 6.7, 6.6% w/v PEG 4000 Resolution 5.50 Å R-free 0.428
3 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain O; UniProt 53–412 Chain P; UniProt 53–412 Chain W; UniProt 53–412 Chain X; UniProt 53–412 Chain o; UniProt 53–412 Chain p; UniProt 53–412 Not recorded Growth/differentiation factor 5 × 2 (P43026) Neogenin × 2 (P97798) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.1 M NaCl, 20 mM MES pH 6.7, 6.6% w/v PEG 4000 Resolution 5.50 Å R-free 0.428

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.

10 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RGMB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 4–363; UniProt 53–412 Author chain D; PDBConstruct 4–363; UniProt 53–412 Author chain I; PDBConstruct 4–363; UniProt 53–412 Author chain J; PDBConstruct 4–363; UniProt 53–412 Author chain O; PDBConstruct 4–363; UniProt 53–412 Author chain P; PDBConstruct 4–363; UniProt 53–412 Author chain S; PDBConstruct 4–363; UniProt 53–412 Author chain T; PDBConstruct 4–363; UniProt 53–412 Author chain U; PDBConstruct 4–363; UniProt 53–412 Author chain V; PDBConstruct 4–363; UniProt 53–412 Author chain W; PDBConstruct 4–363; UniProt 53–412 Author chain X; PDBConstruct 4–363; UniProt 53–412 Author chain c; PDBConstruct 4–363; UniProt 53–412 Author chain d; PDBConstruct 4–363; UniProt 53–412 Author chain i; PDBConstruct 4–363; UniProt 53–412 Author chain j; PDBConstruct 4–363; UniProt 53–412 Author chain o; PDBConstruct 4–363; UniProt 53–412 Author chain p; PDBConstruct 4–363; UniProt 53–412

Neogenin

Mus musculus

UniProt P97798

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain E; UniProt 883–1123 Chain F; UniProt 883–1123 Not recorded Growth/differentiation factor 5 × 2 (P43026) RGM domain family member B × 6 (Q6NW40) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.1 M NaCl, 20 mM MES pH 6.7, 6.6% w/v PEG 4000 Resolution 5.50 Å R-free 0.428
2 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain K; UniProt 883–1123 Chain L; UniProt 883–1123 Not recorded Growth/differentiation factor 5 × 2 (P43026) RGM domain family member B × 6 (Q6NW40) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.1 M NaCl, 20 mM MES pH 6.7, 6.6% w/v PEG 4000 Resolution 5.50 Å R-free 0.428
3 Protein heterocomplex Heteromer Protein × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain Q; UniProt 883–1123 Chain R; UniProt 883–1123 Not recorded Growth/differentiation factor 5 × 2 (P43026) RGM domain family member B × 6 (Q6NW40) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;294 K;0.1 M NaCl, 20 mM MES pH 6.7, 6.6% w/v PEG 4000 Resolution 5.50 Å R-free 0.428

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.

8 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NEO1_MOUSE
Isoform P97798-4
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 4–244; UniProt 883–1123 Author chain F; PDBConstruct 4–244; UniProt 883–1123 Author chain K; PDBConstruct 4–244; UniProt 883–1123 Author chain L; PDBConstruct 4–244; UniProt 883–1123 Author chain Q; PDBConstruct 4–244; UniProt 883–1123 Author chain R; PDBConstruct 4–244; UniProt 883–1123

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 6z3m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6z3m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6z3m
Deposition date deposition_date2020-05-21
Structure title titleRepulsive Guidance Molecule B (RGMB) in complex with Growth Differentiation Factor 5 (GDF5) and Neogenin 1 (NEO1).
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_guinier87.65
Radius of gyration Rg (electron density) rg_electron88.38
Forward intensity I(0) i01862880000.00
Molecular weight molecular_weight359500.0 kDa
Excluded volume excluded_volume447230 ų
Envelope volume envelope_volume920280 ų
Hydration-shell volume shell_volume94925 ų
Envelope diameter envelope_diameter309.5
Shell Rg shell_rg74.22
Envelope Rg envelope_rg82.94
Shape Rg shape_rg88.40
Total Rg total_rg88.09
Total atoms total_atoms25210
Residues n_residues3257
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 dmax230.1
Rg (real space) rg_real84.27
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real1.7930e+09
I(0) uncertainty (real space) i0_real_error3.5740e+07
Rg (reciprocal space) rg_reciprocal86.12
I(0) (reciprocal space) i0_reciprocal1854000000.0000
Solution quality estimate total_estimate0.8919
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary115.0
Skewness Skewness skewness0.018
Kurtosis Kurtosis kurtosis-0.759
Angular range angular_range— – 0.0900 −1
Current regularization parameter α current_alpha1.1160
Highest regularization parameter α highest_alpha42630000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.964; Stabil: 0.965; Sysdev: 1.000; Positv: 1.000; Valcen: 0.811; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)