1rf0

Crystal Structure of Fragment D of gammaE132A Fibrinogen

Method: X-RAY DIFFRACTION Dmax: 203.5 Å Quality: REASONABLE

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

Fibrinogen alpha/alpha-E chain

Homo sapiens

UniProt P02671

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 145–210 Fragment:Fibrinogen alpha/alpha-E Chain Fibrinogen beta chain × 1 (P02675) Fibrinogen gamma chain × 1 (P02679) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;277 K;14-15% PEG 3350, 70 mM calcium chloride, 2 mM sodium azide, 50 mM Tris pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.81 Å R-free 0.286
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 145–210 Fragment:Fibrinogen alpha/alpha-E Chain Fibrinogen beta chain × 1 (P02675) Fibrinogen gamma chain × 1 (P02679) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;277 K;14-15% PEG 3350, 70 mM calcium chloride, 2 mM sodium azide, 50 mM Tris pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.81 Å R-free 0.286

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 68 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIBA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–66; UniProt 145–210 Author chain D; PDBConstruct 1–66; UniProt 145–210

Fibrinogen beta chain

Homo sapiens

UniProt P02675

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 179–491 Fragment:Fibrinogen Bbeta Chain Fibrinogen alpha/alpha-E chain × 1 (P02671) Fibrinogen gamma chain × 1 (P02679) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;277 K;14-15% PEG 3350, 70 mM calcium chloride, 2 mM sodium azide, 50 mM Tris pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.81 Å R-free 0.286
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 179–491 Fragment:Fibrinogen Bbeta Chain Fibrinogen alpha/alpha-E chain × 1 (P02671) Fibrinogen gamma chain × 1 (P02679) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;277 K;14-15% PEG 3350, 70 mM calcium chloride, 2 mM sodium azide, 50 mM Tris pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.81 Å R-free 0.286

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.

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

View Construct and Data Evidence
UniProt name FIBB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–313; UniProt 179–491 Author chain E; PDBConstruct 1–313; UniProt 179–491

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 122–432 Fragment:Fibrinogen gamma chain Mutation:E132A Fibrinogen alpha/alpha-E chain × 1 (P02671) Fibrinogen beta chain × 1 (P02675) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;277 K;14-15% PEG 3350, 70 mM calcium chloride, 2 mM sodium azide, 50 mM Tris pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.81 Å R-free 0.286
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 122–432 Fragment:Fibrinogen gamma chain Mutation:E132A Fibrinogen alpha/alpha-E chain × 1 (P02671) Fibrinogen beta chain × 1 (P02675) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;277 K;14-15% PEG 3350, 70 mM calcium chloride, 2 mM sodium azide, 50 mM Tris pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.81 Å R-free 0.286

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
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–311; UniProt 122–432 Author chain F; PDBConstruct 1–311; UniProt 122–432

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 1rf0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1rf0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1rf0
Deposition date deposition_date2003-11-07
Structure title titleCrystal Structure of Fragment D of gammaE132A Fibrinogen
Keywords keywords;BLOOD COAGULATION, FIBRINOGEN, FIBRINOGEN FRAGMENT D, RECOMBINANT FIBRINOGEN FRAGMENT D, RECOMBINANT FIBRINOGEN gammaE132A, fragment D of gammaE132A fibrinogen, 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_guinier56.03
Radius of gyration Rg (electron density) rg_electron57.48
Forward intensity I(0) i0359230000.00
Molecular weight molecular_weight151690.0 kDa
Excluded volume excluded_volume187350 ų
Envelope volume envelope_volume264470 ų
Hydration-shell volume shell_volume44649 ų
Envelope diameter envelope_diameter216.1
Shell Rg shell_rg47.61
Envelope Rg envelope_rg56.82
Shape Rg shape_rg57.49
Total Rg total_rg57.12
Total atoms total_atoms10656
Residues n_residues1323
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 dmax203.5
Rg (real space) rg_real59.39
Rg uncertainty (real space) rg_real_error0.96
I(0) (real space) i0_real3.6190e+08
I(0) uncertainty (real space) i0_real_error6.0980e+06
Rg (reciprocal space) rg_reciprocal55.15
I(0) (reciprocal space) i0_reciprocal358200000.0000
Solution quality estimate total_estimate0.5088
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary36.3
Skewness Skewness skewness0.613
Kurtosis Kurtosis kurtosis-0.392
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha1.4960
Highest regularization parameter α highest_alpha8317000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.494; Stabil: 0.918; Sysdev: 0.000; Positv: 1.000; Valcen: 0.266; Smooth: 0.117

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 23 domains

SCOP 2.08 (10 domains)

Domain ID domain_idd1rf0a_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.8 — Fibrinogen coiled-coil and central regions
Family Family familyh.1.8.1 — Fibrinogen coiled-coil and central regions
Domain ID domain_idd1rf0b1
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_idd1rf0b2
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.8 — Fibrinogen coiled-coil and central regions
Family Family familyh.1.8.1 — Fibrinogen coiled-coil and central regions
Domain ID domain_idd1rf0c1
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_idd1rf0c2
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.8 — Fibrinogen coiled-coil and central regions
Family Family familyh.1.8.1 — Fibrinogen coiled-coil and central regions
Domain ID domain_idd1rf0d_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.8 — Fibrinogen coiled-coil and central regions
Family Family familyh.1.8.1 — Fibrinogen coiled-coil and central regions
Domain ID domain_idd1rf0e1
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_idd1rf0e2
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.8 — Fibrinogen coiled-coil and central regions
Family Family familyh.1.8.1 — Fibrinogen coiled-coil and central regions
Domain ID domain_idd1rf0f1
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_idd1rf0f2
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.8 — Fibrinogen coiled-coil and central regions
Family Family familyh.1.8.1 — Fibrinogen coiled-coil and central regions

CATH v4.4 (13 domains)

Domain ID domain_id1rf0A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily50
Domain ID domain_id1rf0B01
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_id1rf0B02
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_id1rf0C01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily50
Domain ID domain_id1rf0C02
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_id1rf0C03
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_id1rf0D00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily50
Domain ID domain_id1rf0E01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily50
Domain ID domain_id1rf0E02
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_id1rf0E03
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_id1rf0F01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily50
Domain ID domain_id1rf0F02
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_id1rf0F03
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)