3hms

Crystal Crystal structure of the N-terminal fragment (28-126) of the human hepatocyte growth factor/scatter factor, orthorhombic crystal form

Method: X-RAY DIFFRACTION Dmax: 43.7 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 28–126 Fragment:N-terminal domain: UNP residues 28-126 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;50 mM Ammonium sulfate, 28-32% PEG 1000 or 2000, 50 mM Tris-HCl pH 8.0, 5% Isopropanol, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.70 Å R-free 0.255

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 3–101; UniProt 28–126

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 3hms

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3hms
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3hms
Deposition date deposition_date2009-05-29
Structure title titleCrystal Crystal structure of the N-terminal fragment (28-126) of the human hepatocyte growth factor/scatter factor, orthorhombic crystal form
Keywords keywords;HGF/SF, hormone/growth factor, Disulfide bond, Glycoprotein, Growth factor, Kringle, Pyrrolidone carboxylic acid, Serine protease homolog, HORMONE ;; HORMONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier13.68
Radius of gyration Rg (electron density) rg_electron12.28
Forward intensity I(0) i02417960.00
Molecular weight molecular_weight10744.0 kDa
Excluded volume excluded_volume13495 ų
Envelope volume envelope_volume14915 ų
Hydration-shell volume shell_volume10294 ų
Envelope diameter envelope_diameter43.4
Shell Rg shell_rg18.09
Envelope Rg envelope_rg12.74
Shape Rg shape_rg12.23
Total Rg total_rg13.78
Total atoms total_atoms753
Residues n_residues91
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 dmax43.7
Rg (real space) rg_real13.59
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real2.4180e+06
I(0) uncertainty (real space) i0_real_error2.3860e+04
Rg (reciprocal space) rg_reciprocal13.59
I(0) (reciprocal space) i0_reciprocal2418000.0000
Solution quality estimate total_estimate0.8111
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.3
Skewness Skewness skewness0.137
Kurtosis Kurtosis kurtosis-0.349
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha681800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.848; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3hmsa_
Class classg — Small proteins
Fold Fold foldg.10 — Hairpin loop containing domain-like
Superfamily Superfamily superfamilyg.10.1 — Hairpin loop containing domain-like
Family Family familyg.10.1.1 — Hairpin loop containing domain

CATH v4.4 (1 domains)

Domain ID domain_id3hmsA00
Class class3 — Alpha Beta
Architecture architecture50 — 3-Layer(bba) Sandwich
Topology topology4 — Hepatocyte Growth Factor
Homologous superfamily homologous superfamily10 — Hepatocyte Growth Factor

8. Citations (1)

9. Files and Curves (10)