1fib

RECOMBINANT HUMAN GAMMA-FIBRINOGEN CARBOXYL TERMINAL FRAGMENT (RESIDUES 143-411) BOUND TO CALCIUM AT PH 6.0

Method: X-RAY DIFFRACTION Dmax: 58.9 Å Quality: GOOD

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

GAMMA-FIBRINOGEN CARBOXYL TERMINAL FRAGMENT

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 Fragment:CARBOXYL TERMINUS, RESIDUES 143 - 411 CA CALCIUM ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.10 Å R-free 0.227

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

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 1fib

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1fib
Deposition date deposition_date1996-04-02
Structure title titleRECOMBINANT HUMAN GAMMA-FIBRINOGEN CARBOXYL TERMINAL FRAGMENT (RESIDUES 143-411) BOUND TO CALCIUM AT PH 6.0
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_guinier18.52
Radius of gyration Rg (electron density) rg_electron17.41
Forward intensity I(0) i014478600.00
Molecular weight molecular_weight28227.0 kDa
Excluded volume excluded_volume35018 ų
Envelope volume envelope_volume39021 ų
Hydration-shell volume shell_volume18519 ų
Envelope diameter envelope_diameter61.7
Shell Rg shell_rg23.91
Envelope Rg envelope_rg17.73
Shape Rg shape_rg17.38
Total Rg total_rg18.45
Total atoms total_atoms1996
Residues n_residues249
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_real18.42
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real1.4480e+07
I(0) uncertainty (real space) i0_real_error1.6210e+05
Rg (reciprocal space) rg_reciprocal18.44
I(0) (reciprocal space) i0_reciprocal14480000.0000
Solution quality estimate total_estimate0.8117
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.216
Kurtosis Kurtosis kurtosis-0.287
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3851000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1fiba_
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 (2 domains)

Domain ID domain_id1fibA01
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_id1fibA02
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)