4m8n

Crystal Structure of PlexinC1/Rap1B Complex

Method: X-RAY DIFFRACTION Dmax: 183.5 Å Quality: GOOD

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

PlexinC1 Intracellular Region

Danio rerio

UniProt Q5RGW1

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 455–1050 Chain D; UniProt 455–1050 Not recorded Ras-related protein Rap-1b × 2 (P61224) MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 AF3 ALUMINUM FLUORIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.3;294.15 K;0.1 M HEPES, 5% 2-propanol, 25% PEG 3350, 3.6% polypropylene glycol P400, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 294.15K Resolution 3.29 Å R-free 0.299
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 455–1050 Chain C; UniProt 455–1050 Not recorded Ras-related protein Rap-1b × 2 (P61224) MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 AF3 ALUMINUM FLUORIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.3;294.15 K;0.1 M HEPES, 5% 2-propanol, 25% PEG 3350, 3.6% polypropylene glycol P400, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 294.15K Resolution 3.29 Å R-free 0.299

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 Q5RGW1_DANRE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–599; UniProt 455–1050 Author chain B; PDBConstruct 4–599; UniProt 455–1050 Author chain C; PDBConstruct 4–599; UniProt 455–1050 Author chain D; PDBConstruct 4–599; UniProt 455–1050

Ras-related protein Rap-1b

Homo sapiens

UniProt P61224

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 E; UniProt 1–166 Chain H; UniProt 1–166 Not recorded PlexinC1 Intracellular Region × 2 (Q5RGW1) MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 AF3 ALUMINUM FLUORIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.3;294.15 K;0.1 M HEPES, 5% 2-propanol, 25% PEG 3350, 3.6% polypropylene glycol P400, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 294.15K Resolution 3.29 Å R-free 0.299
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 1–166 Chain G; UniProt 1–166 Not recorded PlexinC1 Intracellular Region × 2 (Q5RGW1) MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 AF3 ALUMINUM FLUORIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.3;294.15 K;0.1 M HEPES, 5% 2-propanol, 25% PEG 3350, 3.6% polypropylene glycol P400, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 294.15K Resolution 3.29 Å R-free 0.299

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.

22 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAP1B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 4–169; UniProt 1–166 Author chain F; PDBConstruct 4–169; UniProt 1–166 Author chain G; PDBConstruct 4–169; UniProt 1–166 Author chain H; PDBConstruct 4–169; UniProt 1–166

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 4m8n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4m8n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4m8n
Deposition date deposition_date2013-08-13
Structure title titleCrystal Structure of PlexinC1/Rap1B Complex
Keywords keywordsGTPase, GTPase activating protein, Rap, GTP binding, Magnesium Binding, Membrane, 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_guinier54.22
Radius of gyration Rg (electron density) rg_electron53.76
Forward intensity I(0) i01364540000.00
Molecular weight molecular_weight315280.0 kDa
Excluded volume excluded_volume396620 ų
Envelope volume envelope_volume576260 ų
Hydration-shell volume shell_volume89367 ų
Envelope diameter envelope_diameter180.7
Shell Rg shell_rg57.00
Envelope Rg envelope_rg52.31
Shape Rg shape_rg53.77
Total Rg total_rg53.84
Total atoms total_atoms22218
Residues n_residues2934
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 dmax183.5
Rg (real space) rg_real54.28
Rg uncertainty (real space) rg_real_error1.49
I(0) (real space) i0_real1.3650e+09
I(0) uncertainty (real space) i0_real_error2.6520e+07
Rg (reciprocal space) rg_reciprocal54.15
I(0) (reciprocal space) i0_reciprocal1364000000.0000
Solution quality estimate total_estimate0.8217
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.3
Skewness Skewness skewness0.324
Kurtosis Kurtosis kurtosis-0.500
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha108500000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.893; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id4m8nA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology506 — GTPase Activation - p120GAP; domain 1
Homologous superfamily homologous superfamily10 — GTPase Activation - p120gap; domain 1
Domain ID domain_id4m8nA02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id4m8nB01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology506 — GTPase Activation - p120GAP; domain 1
Homologous superfamily homologous superfamily10 — GTPase Activation - p120gap; domain 1
Domain ID domain_id4m8nB02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id4m8nC01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology506 — GTPase Activation - p120GAP; domain 1
Homologous superfamily homologous superfamily10 — GTPase Activation - p120gap; domain 1
Domain ID domain_id4m8nC02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id4m8nD01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology506 — GTPase Activation - p120GAP; domain 1
Homologous superfamily homologous superfamily10 — GTPase Activation - p120gap; domain 1
Domain ID domain_id4m8nD02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Domain ID domain_id4m8nE00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id4m8nF00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id4m8nG00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id4m8nH00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)