9khc

Crystal structure of wild-type human fibrinogen gamma chain C-terminal domain (gamma-nodule) complexed with GPRP peptide

Method: X-RAY DIFFRACTION Dmax: 92.9 Å Quality: GOOD

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

Isoform Gamma-A of Fibrinogen gamma chain

Homo sapiens

UniProt P02679

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 169–437 Not recorded GLY-PRO-ARG-PRO × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;The reservoir solution contains 0.1 M MES pH 6.0, 20% PEG8000, and 70 mM CaCl2. After clystals were grown, the reservoir solution containing 20 mM GPRP was added to the drop. Resolution 1.32 Å R-free 0.203
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 169–437 Not recorded GLY-PRO-ARG-PRO × 1 CA CALCIUM ION × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;The reservoir solution contains 0.1 M MES pH 6.0, 20% PEG8000, and 70 mM CaCl2. After clystals were grown, the reservoir solution containing 20 mM GPRP was added to the drop. Resolution 1.32 Å R-free 0.203

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.

36 other PDB entries and 56 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIBG_HUMAN
Isoform P02679-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–273; UniProt 169–437 Author chain C; PDBConstruct 5–273; UniProt 169–437

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 9khc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9khc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9khc
Deposition date deposition_date2024-11-10
最后修订 last_revision2025-11-12
Structure title titleCrystal structure of wild-type human fibrinogen gamma chain C-terminal domain (gamma-nodule) complexed with GPRP peptide
Keywords keywordsfibrinogen, fibrin formation, hemostasis, coagulation factor, 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_guinier28.22
Radius of gyration Rg (electron density) rg_electron27.55
Forward intensity I(0) i055019200.00
Molecular weight molecular_weight57268.0 kDa
Excluded volume excluded_volume71040 ų
Envelope volume envelope_volume83035 ų
Hydration-shell volume shell_volume26048 ų
Envelope diameter envelope_diameter97.3
Shell Rg shell_rg33.65
Envelope Rg envelope_rg27.37
Shape Rg shape_rg27.55
Total Rg total_rg28.14
Total atoms total_atoms4048
Residues n_residues504
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 dmax92.9
Rg (real space) rg_real28.40
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real5.5020e+07
I(0) uncertainty (real space) i0_real_error8.2720e+05
Rg (reciprocal space) rg_reciprocal28.35
I(0) (reciprocal space) i0_reciprocal55020000.0000
Solution quality estimate total_estimate0.8570
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.9
Skewness Skewness skewness0.393
Kurtosis Kurtosis kurtosis-0.621
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9024000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.814; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.808; Smooth: 0.888

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)