4ui0

Crystal structure of the human RGMB-BMP2 complex, crystal form 2

Method: X-RAY DIFFRACTION Dmax: 79.6 Å Quality: REASONABLE

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

BONE MORPHOGENETIC PROTEIN 2

HOMO SAPIENS

UniProt P12643

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 283–396 Chain B; UniProt 283–396 Fragment:C-TERMINAL DOMAIN SIGNALING DOMAIN, RESIDUES 283-396 RGM DOMAIN FAMILY MEMBER B × 1 (Q6NW40) MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 FLC CITRATE ANION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4;0.08 M CITRIC ACID PH 4.0, 15% (V/V) MPD Resolution 2.80 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.

19 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BMP2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–114; UniProt 283–396 Author chain B; PDBConstruct 1–114; UniProt 283–396

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 53–136 Fragment:N-TERMINAL DOMAIN, RESIDUES 53-136 BONE MORPHOGENETIC PROTEIN 2 × 2 (P12643) MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 FLC CITRATE ANION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4;0.08 M CITRIC ACID PH 4.0, 15% (V/V) MPD Resolution 2.80 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.

10 other PDB entries and 14 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 4–87; UniProt 53–136

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 4ui0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4ui0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4ui0
Deposition date deposition_date2015-03-27
Structure title titleCrystal structure of the human RGMB-BMP2 complex, crystal form 2
Keywords keywords;SIGNALING PROTEIN, REPULSIVE GUIDANCE MOLECULE, BONE MORPHOGENETIC PROTEIN PATHWAY, HEMOJUVELIN, MORPHOGEN, AXON GUIDANCE, CELL SURFACE RECEPTOR SIGNALING ;; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.95
Radius of gyration Rg (electron density) rg_electron21.70
Forward intensity I(0) i016229500.00
Molecular weight molecular_weight29262.0 kDa
Excluded volume excluded_volume36149 ų
Envelope volume envelope_volume45382 ų
Hydration-shell volume shell_volume18452 ų
Envelope diameter envelope_diameter81.5
Shell Rg shell_rg27.23
Envelope Rg envelope_rg22.24
Shape Rg shape_rg21.75
Total Rg total_rg22.34
Total atoms total_atoms2040
Residues n_residues261
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 dmax79.6
Rg (real space) rg_real22.13
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real1.6230e+07
I(0) uncertainty (real space) i0_real_error2.0510e+05
Rg (reciprocal space) rg_reciprocal22.10
I(0) (reciprocal space) i0_reciprocal16230000.0000
Solution quality estimate total_estimate0.6225
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.6
Skewness Skewness skewness0.579
Kurtosis Kurtosis kurtosis0.030
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3296000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.654; Stabil: 1.000; Sysdev: 0.145; Positv: 1.000; Valcen: 0.702; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4ui0a_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.2 — Transforming growth factor (TGF)-beta
Domain ID domain_idd4ui0b_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.2 — Transforming growth factor (TGF)-beta

CATH v4.4 (2 domains)

Domain ID domain_id4ui0A00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id4ui0B00
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)