8ol9

Anti-FIXa Fab in complex with human des-(Gla-EGF1) FIXa

Method: X-RAY DIFFRACTION Dmax: 130.2 Å Quality: REASONABLE

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

Coagulation factor IX heavy chain

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain H; UniProt 227–461 Chain L; UniProt 131–188 Not recorded Light chain of FIXa binding Fab × 1 Heavy chain of FIXa binding Fab × 1 SO4 SULFATE ION × 2 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 CA CALCIUM ION × 1 0GJ L-alpha-glutamyl-N-{(1S)-4-{[amino(iminio)methyl]amino}-1-[(1S)-2-chloro-1-hydroxyethyl]butyl}glycinamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;291 K;0.5 M ammonium sulphate, 0.1 M sodium citrate, pH 5.6, !.0 M lithium sulphate Resolution 2.60 Å R-free 0.323

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 3, 4
Chains and sequence ranges Author chain H; PDBConstruct 1–235; UniProt 227–461 Author chain L; PDBConstruct 2–59; UniProt 131–188

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 8ol9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ol9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ol9
Deposition date deposition_date2023-03-30
Structure title titleAnti-FIXa Fab in complex with human des-(Gla-EGF1) FIXa
Keywords keywordsFab, FIXa, BLOOD CLOTTING; BLOOD CLOTTING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.01
Radius of gyration Rg (electron density) rg_electron36.29
Forward intensity I(0) i0195402000.00
Molecular weight molecular_weight74234.0 kDa
Excluded volume excluded_volume71253 ų
Envelope volume envelope_volume132840 ų
Hydration-shell volume shell_volume33810 ų
Envelope diameter envelope_diameter126.2
Shell Rg shell_rg38.35
Envelope Rg envelope_rg36.25
Shape Rg shape_rg36.26
Total Rg total_rg36.44
Total atoms total_atoms5603
Residues n_residues724
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 dmax130.2
Rg (real space) rg_real36.50
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real1.9540e+08
I(0) uncertainty (real space) i0_real_error3.1820e+06
Rg (reciprocal space) rg_reciprocal36.20
I(0) (reciprocal space) i0_reciprocal195300000.0000
Solution quality estimate total_estimate0.6976
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.6
Skewness Skewness skewness0.587
Kurtosis Kurtosis kurtosis-0.412
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha14710000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.551; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.410; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id8ol9A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8ol9A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8ol9B01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8ol9B02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)