1dug

STRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING AND FACTOR XIIIA CROSSLINKING SITES OBTAINED THROUGH CARRIER PROTEIN DRIVEN CRYSTALLIZATION

Method: X-RAY DIFFRACTION Dmax: 67.7 Å Quality: EXCELLENT

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

chimera of GLUTATHIONE S-TRANSFERASE-synthetic LINKEr-C-TERMINAL 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 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 424–437 Chain B; UniProt 424–437 Not recorded GSH Glutathione × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;277 K;PEG 3350, sodium acetate, sodium chloride, ammonium sulfate, Tris, reduced glutathione, pH 4.6, VAPOR DIFFUSION, HANGING DROP Resolution 1.80 Å R-free 0.226

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 221–234; UniProt 424–437 Author chain B; PDBConstruct 221–234; UniProt 424–437

chimera of GLUTATHIONE S-TRANSFERASE-synthetic LINKEr-C-TERMINAL FIBRINOGEN GAMMA CHAIN

Homo sapiens

UniProt P08515

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–218 Chain B; UniProt 2–218 Not recorded GSH Glutathione × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.6;277 K;PEG 3350, sodium acetate, sodium chloride, ammonium sulfate, Tris, reduced glutathione, pH 4.6, VAPOR DIFFUSION, HANGING DROP Resolution 1.80 Å R-free 0.226

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.

64 other PDB entries and 70 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GT26_SCHJA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–217; UniProt 2–218 Author chain B; PDBConstruct 1–217; UniProt 2–218

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 1dug

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1dug
Deposition date deposition_date2000-01-17
Structure title titleSTRUCTURE OF THE FIBRINOGEN G CHAIN INTEGRIN BINDING AND FACTOR XIIIA CROSSLINKING SITES OBTAINED THROUGH CARRIER PROTEIN DRIVEN CRYSTALLIZATION
Keywords keywordsgamma chain integrin fragment, carrier protein driven crystallization, transferase, blood clotting; transferase, blood clotting
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.13
Radius of gyration Rg (electron density) rg_electron21.88
Forward intensity I(0) i046673100.00
Molecular weight molecular_weight54795.0 kDa
Excluded volume excluded_volume69241 ų
Envelope volume envelope_volume80178 ų
Hydration-shell volume shell_volume29288 ų
Envelope diameter envelope_diameter70.0
Shell Rg shell_rg29.69
Envelope Rg envelope_rg21.89
Shape Rg shape_rg21.88
Total Rg total_rg22.79
Total atoms total_atoms3858
Residues n_residues468
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 dmax67.7
Rg (real space) rg_real22.95
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real4.6670e+07
I(0) uncertainty (real space) i0_real_error5.8530e+05
Rg (reciprocal space) rg_reciprocal22.99
I(0) (reciprocal space) i0_reciprocal46670000.0000
Solution quality estimate total_estimate0.9114
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.2
Skewness Skewness skewness0.090
Kurtosis Kurtosis kurtosis-0.527
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22870000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.957; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1duga1
Class classa — All alpha proteins
Fold Fold folda.45 — GST C-terminal domain-like
Superfamily Superfamily superfamilya.45.1 — GST C-terminal domain-like
Family Family familya.45.1.1 — Glutathione S-transferase (GST), C-terminal domain
Domain ID domain_idd1duga2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.5 — Glutathione S-transferase (GST), N-terminal domain
Domain ID domain_idd1dugb1
Class classa — All alpha proteins
Fold Fold folda.45 — GST C-terminal domain-like
Superfamily Superfamily superfamilya.45.1 — GST C-terminal domain-like
Family Family familya.45.1.1 — Glutathione S-transferase (GST), C-terminal domain
Domain ID domain_idd1dugb2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.5 — Glutathione S-transferase (GST), N-terminal domain

CATH v4.4 (4 domains)

Domain ID domain_id1dugA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id1dugA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1050 — Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Homologous superfamily homologous superfamily10
Domain ID domain_id1dugB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id1dugB02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1050 — Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)