1edm

EPIDERMAL GROWTH FACTOR-LIKE DOMAIN FROM HUMAN FACTOR IX

Method: X-RAY DIFFRACTION Dmax: 45.3 Å Quality: GOOD

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

FACTOR IX

Homo sapiens

UniProt P00740

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 92–130 Chain C; UniProt 92–130 Fragment:EPIDERMAL GROWTH FACTOR-LIKE DOMAIN CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.3;pH 7.3 Resolution 1.50 Å

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.

55 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FA9_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–39; UniProt 92–130 Author chain C; PDBConstruct 1–39; UniProt 92–130

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 1edm

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1edm
Deposition date deposition_date1996-03-21
Structure title titleEPIDERMAL GROWTH FACTOR-LIKE DOMAIN FROM HUMAN FACTOR IX
Keywords keywordsEPIDERMAL GROWTH FACTOR, EGF, CALCIUM-BINDING, EGF-LIKE DOMAIN, STRUCTURE AND FUNCTION, HUMAN FACTOR IX, COAGULATION FACTOR; COAGULATION FACTOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier13.65
Radius of gyration Rg (electron density) rg_electron13.47
Forward intensity I(0) i01781300.00
Molecular weight molecular_weight7918.0 kDa
Excluded volume excluded_volume9273 ų
Envelope volume envelope_volume11091 ų
Hydration-shell volume shell_volume7644 ų
Envelope diameter envelope_diameter45.4
Shell Rg shell_rg17.75
Envelope Rg envelope_rg13.84
Shape Rg shape_rg13.52
Total Rg total_rg14.25
Total atoms total_atoms540
Residues n_residues78
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 dmax45.3
Rg (real space) rg_real13.67
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real1.7810e+06
I(0) uncertainty (real space) i0_real_error1.7840e+04
Rg (reciprocal space) rg_reciprocal13.67
I(0) (reciprocal space) i0_reciprocal1781000.0000
Solution quality estimate total_estimate0.8919
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary13.2
Skewness Skewness skewness0.249
Kurtosis Kurtosis kurtosis-0.589
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha181100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.854; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1edmb_
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.11 — EGF/Laminin
Family Family familyg.3.11.1 — EGF-type module
Domain ID domain_idd1edmc_
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.11 — EGF/Laminin
Family Family familyg.3.11.1 — EGF-type module

8. Citations (2)

9. Files and Curves (10)