9khb

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

Method: X-RAY DIFFRACTION Dmax: 58.9 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 169–437 Not recorded GOL GLYCEROL × 3 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;Reservoir solution (22% PEG 8000, 150 mM 2-Morpholinoethanesulfonic acid, pH 6.0, 70 mM calcium choride) Protein solution (20 mM 2-[4-(2-Hydroxyethyl)-1-piperazinyl]ethanesulfonic acid, pH7.4, 120 mM sodium choride, 70 mM calcium choride) Resolution 1.03 Å R-free 0.139

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 57 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

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 9khb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9khb
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)
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_guinier18.27
Radius of gyration Rg (electron density) rg_electron17.21
Forward intensity I(0) i014713100.00
Molecular weight molecular_weight28606.0 kDa
Excluded volume excluded_volume35522 ų
Envelope volume envelope_volume38268 ų
Hydration-shell volume shell_volume18318 ų
Envelope diameter envelope_diameter61.4
Shell Rg shell_rg23.77
Envelope Rg envelope_rg17.56
Shape Rg shape_rg17.18
Total Rg total_rg18.25
Total atoms total_atoms3903
Residues n_residues250
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 dmax58.9
Rg (real space) rg_real18.17
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real1.4710e+07
I(0) uncertainty (real space) i0_real_error1.6620e+05
Rg (reciprocal space) rg_reciprocal18.19
I(0) (reciprocal space) i0_reciprocal14710000.0000
Solution quality estimate total_estimate0.8845
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.9
Skewness Skewness skewness0.213
Kurtosis Kurtosis kurtosis-0.293
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4111000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.842; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.975

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)