1fze

CRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN

Method: X-RAY DIFFRACTION Dmax: 212.4 Å Quality: REASONABLE

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

FIBRINOGEN

OrganismNot specified

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 130–216 Chain D; UniProt 130–216 Fragment:FRAGMENT D FIBRINOGEN × 2 (P02675) FIBRINOGEN × 2 (P02679) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 CA CALCIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 3.00 Å R-free 0.318
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 130–216 Fragment:FRAGMENT D FIBRINOGEN × 1 (P02675) FIBRINOGEN × 1 (P02679) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 3.00 Å R-free 0.318
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 130–216 Fragment:FRAGMENT D FIBRINOGEN × 1 (P02675) FIBRINOGEN × 1 (P02679) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 3.00 Å R-free 0.318

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 67 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 1–87; UniProt 130–216 Author chain D; PDBConstruct 1–87; UniProt 130–216

FIBRINOGEN

OrganismNot specified

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 164–491 Chain E; UniProt 164–491 Fragment:FRAGMENT D FIBRINOGEN × 2 (P02671) FIBRINOGEN × 2 (P02679) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 CA CALCIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 3.00 Å R-free 0.318
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 164–491 Fragment:FRAGMENT D FIBRINOGEN × 1 (P02671) FIBRINOGEN × 1 (P02679) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 3.00 Å R-free 0.318
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 164–491 Fragment:FRAGMENT D FIBRINOGEN × 1 (P02671) FIBRINOGEN × 1 (P02679) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 3.00 Å R-free 0.318

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 55 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 1–328; UniProt 164–491 Author chain E; PDBConstruct 1–328; UniProt 164–491

FIBRINOGEN

OrganismNot specified

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 115–432 Chain F; UniProt 115–432 Fragment:FRAGMENT D FIBRINOGEN × 2 (P02671) FIBRINOGEN × 2 (P02675) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 CA CALCIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 3.00 Å R-free 0.318
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 115–432 Fragment:FRAGMENT D FIBRINOGEN × 1 (P02671) FIBRINOGEN × 1 (P02675) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 3.00 Å R-free 0.318
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 115–432 Fragment:FRAGMENT D FIBRINOGEN × 1 (P02671) FIBRINOGEN × 1 (P02675) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 3.00 Å R-free 0.318

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 55 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 2–319; UniProt 115–432 Author chain F; PDBConstruct 2–319; UniProt 115–432

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 1fze

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1fze
Deposition date deposition_date1998-12-23
Structure title titleCRYSTAL STRUCTURE OF FRAGMENT DOUBLE-D FROM HUMAN FIBRIN
Keywords keywordsBLOOD COAGULATION, PLASMA, PLATELET, FIBRINOGEN, FIBRIN; BLOOD COAGULATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier58.22
Radius of gyration Rg (electron density) rg_electron61.02
Forward intensity I(0) i0394837000.00
Molecular weight molecular_weight159480.0 kDa
Excluded volume excluded_volume197400 ų
Envelope volume envelope_volume269960 ų
Hydration-shell volume shell_volume45992 ų
Envelope diameter envelope_diameter263.6
Shell Rg shell_rg44.28
Envelope Rg envelope_rg63.92
Shape Rg shape_rg60.86
Total Rg total_rg60.97
Total atoms total_atoms11201
Residues n_residues1383
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 dmax212.4
Rg (real space) rg_real59.43
Rg uncertainty (real space) rg_real_error2.73
I(0) (real space) i0_real3.9430e+08
I(0) uncertainty (real space) i0_real_error8.0210e+06
Rg (reciprocal space) rg_reciprocal56.87
I(0) (reciprocal space) i0_reciprocal393000000.0000
Solution quality estimate total_estimate0.6512
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.3
Skewness Skewness skewness0.742
Kurtosis Kurtosis kurtosis-0.131
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0031
Highest regularization parameter α highest_alpha9884000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.282; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.098; Smooth: 0.522

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (10 domains)

Domain ID domain_idd1fzea_
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_idd1fzeb1
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_idd1fzeb2
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_idd1fzec1
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_idd1fzec2
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_idd1fzed_
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_idd1fzee1
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_idd1fzee2
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_idd1fzef1
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_idd1fzef2
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 (10 domains)

Domain ID domain_id1fzeA00
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_id1fzeB01
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_id1fzeB02
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_id1fzeC01
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_id1fzeC02
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_id1fzeD00
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_id1fzeE01
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_id1fzeE02
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_id1fzeF01
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_id1fzeF02
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)