6gcu

MET receptor in complex with InlB internalin domain and DARPin A3A

Method: X-RAY DIFFRACTION Dmax: 182.8 Å Quality: GOOD

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

Hepatocyte growth factor receptor

Homo sapiens

UniProt P08581

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 25–741 Not recorded Internalin B × 1 (P25147) DARPin A3A × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293.15 K;0.1 M HEPES sodium salt pH 7.5, 12% w/v PEG4000, protein complex concentration 5 mg/mL, equimolar ratio of macromolecules, drop size 0.2 uL, protein:reservoir ratio 1:1 Resolution 6.00 Å R-free 0.271
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 25–741 Not recorded Internalin B × 1 (P25147) DARPin A3A × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293.15 K;0.1 M HEPES sodium salt pH 7.5, 12% w/v PEG4000, protein complex concentration 5 mg/mL, equimolar ratio of macromolecules, drop size 0.2 uL, protein:reservoir ratio 1:1 Resolution 6.00 Å R-free 0.271

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.

128 other PDB entries and 165 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MET_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–720; UniProt 25–741 Author chain D; PDBConstruct 4–720; UniProt 25–741

Internalin B

Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)

UniProt P25147

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 B; UniProt 36–321 Not recorded Hepatocyte growth factor receptor × 1 (P08581) DARPin A3A × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293.15 K;0.1 M HEPES sodium salt pH 7.5, 12% w/v PEG4000, protein complex concentration 5 mg/mL, equimolar ratio of macromolecules, drop size 0.2 uL, protein:reservoir ratio 1:1 Resolution 6.00 Å R-free 0.271
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 36–321 Not recorded Hepatocyte growth factor receptor × 1 (P08581) DARPin A3A × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293.15 K;0.1 M HEPES sodium salt pH 7.5, 12% w/v PEG4000, protein complex concentration 5 mg/mL, equimolar ratio of macromolecules, drop size 0.2 uL, protein:reservoir ratio 1:1 Resolution 6.00 Å R-free 0.271

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.

16 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INLB_LISMO
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–289; UniProt 36–321 Author chain E; PDBConstruct 4–289; UniProt 36–321

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 6gcu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6gcu
Deposition date deposition_date2018-04-19
Structure title titleMET receptor in complex with InlB internalin domain and DARPin A3A
Keywords keywordsreceptor tyrosine kinase, bacterial invasion protein, artificial binding protein, 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_guinier52.58
Radius of gyration Rg (electron density) rg_electron52.26
Forward intensity I(0) i0885049000.00
Molecular weight molecular_weight247960.0 kDa
Excluded volume excluded_volume310500 ų
Envelope volume envelope_volume451430 ų
Hydration-shell volume shell_volume73915 ų
Envelope diameter envelope_diameter180.8
Shell Rg shell_rg52.98
Envelope Rg envelope_rg51.43
Shape Rg shape_rg52.29
Total Rg total_rg52.21
Total atoms total_atoms17448
Residues n_residues2232
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 dmax182.8
Rg (real space) rg_real52.67
Rg uncertainty (real space) rg_real_error2.23
I(0) (real space) i0_real8.8510e+08
I(0) uncertainty (real space) i0_real_error1.7640e+07
Rg (reciprocal space) rg_reciprocal52.49
I(0) (reciprocal space) i0_reciprocal884800000.0000
Solution quality estimate total_estimate0.8854
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary60.9
Skewness Skewness skewness0.306
Kurtosis Kurtosis kurtosis-0.563
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha63030000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.870; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.906

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)