1shy

The Crystal Structure of HGF beta-chain in Complex with the Sema Domain of the Met Receptor.

Method: X-RAY DIFFRACTION Dmax: 104.0 Å Quality: GOOD

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

Hepatocyte growth factor

Homo sapiens

UniProt P14210

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 495–728 Fragment:HGF beta chain Mutation:C604S Hepatocyte growth factor receptor × 1 (P08581) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;292 K;PEG, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 3.22 Å R-free 0.270

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.

35 other PDB entries and 45 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HGF_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–234; UniProt 495–728

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 25–567 Fragment:Met receptor Sema and PSI domain Hepatocyte growth factor × 1 (P14210) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;292 K;PEG, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 292K Resolution 3.22 Å R-free 0.270

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 166 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MET_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–543; UniProt 25–567

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 1shy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1shy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1shy
Deposition date deposition_date2004-02-26
Structure title titleThe Crystal Structure of HGF beta-chain in Complex with the Sema Domain of the Met Receptor.
Keywords keywordsprotease, sema domain, PSI domain, receptor ectodomain growth factor, GROWTH FACTOR-GROWTH FACTOR RECEPTOR COMPLEX; GROWTH FACTOR/GROWTH FACTOR RECEPTOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.91
Radius of gyration Rg (electron density) rg_electron29.09
Forward intensity I(0) i0108204000.00
Molecular weight molecular_weight81600.0 kDa
Excluded volume excluded_volume101880 ų
Envelope volume envelope_volume129900 ų
Hydration-shell volume shell_volume37103 ų
Envelope diameter envelope_diameter114.0
Shell Rg shell_rg36.39
Envelope Rg envelope_rg29.13
Shape Rg shape_rg29.05
Total Rg total_rg29.92
Total atoms total_atoms5735
Residues n_residues727
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 dmax104.0
Rg (real space) rg_real29.88
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real1.0820e+08
I(0) uncertainty (real space) i0_real_error1.6340e+06
Rg (reciprocal space) rg_reciprocal29.90
I(0) (reciprocal space) i0_reciprocal108200000.0000
Solution quality estimate total_estimate0.8742
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.3
Skewness Skewness skewness0.316
Kurtosis Kurtosis kurtosis-0.330
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21460000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.807; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.960

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1shya_
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.2 — Eukaryotic proteases
Domain ID domain_idd1shyb1
Class classb — All beta proteins
Fold Fold foldb.69 — 7-bladed beta-propeller
Superfamily Superfamily superfamilyb.69.12 — Sema domain
Family Family familyb.69.12.1 — Sema domain
Domain ID domain_idd1shyb2
Class classg — Small proteins
Fold Fold foldg.16 — Trefoil/Plexin domain-like
Superfamily Superfamily superfamilyg.16.2 — Plexin repeat
Family Family familyg.16.2.1 — Plexin repeat

CATH v4.4 (4 domains)

Domain ID domain_id1shyA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1shyA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1shyB01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id1shyB02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1680 — ligand-binding face of the semaphorins, domain 2
Homologous superfamily homologous superfamily10 — ligand-binding face of the semaphorins, domain 2

8. Citations (2)

9. Files and Curves (10)