1fic

STRUCTURE OF HUMAN GAMMA FIBRINOGEN 30 KD CARBOXYL TERMINAL FRAGMENT

Method: X-RAY DIFFRACTION Dmax: 94.7 Å Quality: GOOD

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

GAMMA FIBRINOGEN

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 169–437 Chain B; UniProt 169–437 Fragment:30 KD CARBOXYL TERMINAL FRAGMENT CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;pH 6.0 Resolution 2.50 Å R-free 0.244

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
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–269; UniProt 169–437 Author chain B; PDBConstruct 1–269; 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 1fic

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1fic
Deposition date deposition_date1996-08-24
Structure title titleSTRUCTURE OF HUMAN GAMMA FIBRINOGEN 30 KD CARBOXYL TERMINAL FRAGMENT
Keywords keywords;BLOOD COAGULATION, GLYCOPROTEIN, CALCIUM, PLATELET, PLASMA, ALTERNATIVE SPLICING, DISEASE MUTATION, POLYMORPHISM, BLOOD COAGULATION FACTOR ;; BLOOD COAGULATION FACTOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.29
Radius of gyration Rg (electron density) rg_electron25.79
Forward intensity I(0) i058158700.00
Molecular weight molecular_weight58453.0 kDa
Excluded volume excluded_volume72426 ų
Envelope volume envelope_volume86163 ų
Hydration-shell volume shell_volume28225 ų
Envelope diameter envelope_diameter100.1
Shell Rg shell_rg32.48
Envelope Rg envelope_rg26.28
Shape Rg shape_rg25.75
Total Rg total_rg26.60
Total atoms total_atoms4134
Residues n_residues517
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 dmax94.7
Rg (real space) rg_real26.37
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real5.8160e+07
I(0) uncertainty (real space) i0_real_error9.3640e+05
Rg (reciprocal space) rg_reciprocal26.35
I(0) (reciprocal space) i0_reciprocal58160000.0000
Solution quality estimate total_estimate0.8388
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary93.1
Skewness Skewness skewness0.438
Kurtosis Kurtosis kurtosis-0.263
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10710000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.694; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.839; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1fica_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.171 — Fibrinogen C-terminal domain-like
Superfamily Superfamily superfamilyd.171.1 — Fibrinogen C-terminal domain-like
Family Family familyd.171.1.1 — Fibrinogen C-terminal domain-like
Domain ID domain_idd1ficb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.171 — Fibrinogen C-terminal domain-like
Superfamily Superfamily superfamilyd.171.1 — Fibrinogen C-terminal domain-like
Family Family familyd.171.1.1 — Fibrinogen C-terminal domain-like

CATH v4.4 (4 domains)

Domain ID domain_id1ficA01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology215 — Gamma Fibrinogen; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Gamma Fibrinogen, chain A, domain 1
Domain ID domain_id1ficA02
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology530 — Gamma-fibrinogen Carboxyl Terminal Fragment; domain 2
Homologous superfamily homologous superfamily10 — Gamma-fibrinogen Carboxyl Terminal Fragment, domain 2
Domain ID domain_id1ficB01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology215 — Gamma Fibrinogen; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Gamma Fibrinogen, chain A, domain 1
Domain ID domain_id1ficB02
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology530 — Gamma-fibrinogen Carboxyl Terminal Fragment; domain 2
Homologous superfamily homologous superfamily10 — Gamma-fibrinogen Carboxyl Terminal Fragment, domain 2

8. Citations (1)

9. Files and Curves (10)