4uhy

Crystal structure of the human RGMA-BMP2 complex

Method: X-RAY DIFFRACTION Dmax: 79.9 Å Quality: GOOD

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 REPULSIVE GUIDANCE MOLECULE A × 1 (Q96B86) X-RAY DIFFRACTION X-ray crystallization conditions:pH 4;0.1 M CITRIC ACID, PH 4.0, 20% (V/V) 2-METHYL-2,4-PENTANEDIOL (MPD), 0.2 M GLYCINE Resolution 3.20 Å R-free 0.264

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

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 45–140 Fragment:N-TERMINAL DOMAIN, RESIDUES 45-140 BONE MORPHOGENETIC PROTEIN 2 × 2 (P12643) X-RAY DIFFRACTION X-ray crystallization conditions:pH 4;0.1 M CITRIC ACID, PH 4.0, 20% (V/V) 2-METHYL-2,4-PENTANEDIOL (MPD), 0.2 M GLYCINE Resolution 3.20 Å R-free 0.264

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
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 3–98; UniProt 45–140

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 4uhy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4uhy
Deposition date deposition_date2015-03-27
Structure title titleCrystal structure of the human RGMA-BMP2 complex
Keywords keywordsSIGNALING PROTEIN, 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_guinier22.14
Radius of gyration Rg (electron density) rg_electron21.86
Forward intensity I(0) i017170600.00
Molecular weight molecular_weight30222.0 kDa
Excluded volume excluded_volume37319 ų
Envelope volume envelope_volume46639 ų
Hydration-shell volume shell_volume18799 ų
Envelope diameter envelope_diameter81.3
Shell Rg shell_rg27.42
Envelope Rg envelope_rg22.40
Shape Rg shape_rg21.90
Total Rg total_rg22.50
Total atoms total_atoms2112
Residues n_residues273
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 dmax79.9
Rg (real space) rg_real22.32
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real1.7170e+07
I(0) uncertainty (real space) i0_real_error2.0780e+05
Rg (reciprocal space) rg_reciprocal22.28
I(0) (reciprocal space) i0_reciprocal17170000.0000
Solution quality estimate total_estimate0.8264
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.7
Skewness Skewness skewness0.568
Kurtosis Kurtosis kurtosis0.025
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2971000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.673; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.733; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4uhyA00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id4uhyB00
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)