2hod

Crystal Structure of Fragment D from Human Fibrinogen Complexed with Gly-hydroxyPro-Arg-Pro-amide

Method: X-RAY DIFFRACTION Dmax: 219.0 Å Quality: GOOD

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

Fibrinogen alpha chain

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 130–216 Not recorded Fibrinogen beta chain × 1 (P02675) Fibrinogen, gamma polypeptide × 1 (Q53Y18) Gly-hydroxyPro-Arg-Pro-amide peptide ligand × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;equal volumes of 10 mg/ml fragment D, 5 mM Gly-hydroxyPro-Arg-Pro-amide, 50 mM Tris, pH 7.0 and 16% PEG 3350, 50 mM Tris pH 8.0 mM 20 mM CaCl2, 2 mM sodium azide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.90 Å R-free 0.347
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 130–216 Not recorded Fibrinogen beta chain × 1 (P02675) Fibrinogen, gamma polypeptide × 1 (Q53Y18) Gly-hydroxyPro-Arg-Pro-amide peptide ligand × 2 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 7.5;295 K;equal volumes of 10 mg/ml fragment D, 5 mM Gly-hydroxyPro-Arg-Pro-amide, 50 mM Tris, pH 7.0 and 16% PEG 3350, 50 mM Tris pH 8.0 mM 20 mM CaCl2, 2 mM sodium azide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.90 Å R-free 0.347
3 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 130–216 Not recorded Fibrinogen beta chain × 1 (P02675) Fibrinogen, gamma polypeptide × 1 (Q53Y18) Gly-hydroxyPro-Arg-Pro-amide peptide ligand × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;equal volumes of 10 mg/ml fragment D, 5 mM Gly-hydroxyPro-Arg-Pro-amide, 50 mM Tris, pH 7.0 and 16% PEG 3350, 50 mM Tris pH 8.0 mM 20 mM CaCl2, 2 mM sodium azide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.90 Å R-free 0.347
4 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain J; UniProt 130–216 Not recorded Fibrinogen beta chain × 1 (P02675) Fibrinogen, gamma polypeptide × 1 (Q53Y18) Gly-hydroxyPro-Arg-Pro-amide peptide ligand × 2 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 7.5;295 K;equal volumes of 10 mg/ml fragment D, 5 mM Gly-hydroxyPro-Arg-Pro-amide, 50 mM Tris, pH 7.0 and 16% PEG 3350, 50 mM Tris pH 8.0 mM 20 mM CaCl2, 2 mM sodium azide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.90 Å R-free 0.347

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 66 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 Author chain G; PDBConstruct 1–87; UniProt 130–216 Author chain J; PDBConstruct 1–87; UniProt 130–216

Fibrinogen beta chain

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 164–491 Not recorded Fibrinogen alpha chain × 1 (P02671) Fibrinogen, gamma polypeptide × 1 (Q53Y18) Gly-hydroxyPro-Arg-Pro-amide peptide ligand × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;equal volumes of 10 mg/ml fragment D, 5 mM Gly-hydroxyPro-Arg-Pro-amide, 50 mM Tris, pH 7.0 and 16% PEG 3350, 50 mM Tris pH 8.0 mM 20 mM CaCl2, 2 mM sodium azide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.90 Å R-free 0.347
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 164–491 Not recorded Fibrinogen alpha chain × 1 (P02671) Fibrinogen, gamma polypeptide × 1 (Q53Y18) Gly-hydroxyPro-Arg-Pro-amide peptide ligand × 2 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 7.5;295 K;equal volumes of 10 mg/ml fragment D, 5 mM Gly-hydroxyPro-Arg-Pro-amide, 50 mM Tris, pH 7.0 and 16% PEG 3350, 50 mM Tris pH 8.0 mM 20 mM CaCl2, 2 mM sodium azide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.90 Å R-free 0.347
3 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain H; UniProt 164–491 Not recorded Fibrinogen alpha chain × 1 (P02671) Fibrinogen, gamma polypeptide × 1 (Q53Y18) Gly-hydroxyPro-Arg-Pro-amide peptide ligand × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;equal volumes of 10 mg/ml fragment D, 5 mM Gly-hydroxyPro-Arg-Pro-amide, 50 mM Tris, pH 7.0 and 16% PEG 3350, 50 mM Tris pH 8.0 mM 20 mM CaCl2, 2 mM sodium azide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.90 Å R-free 0.347
4 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain K; UniProt 164–491 Not recorded Fibrinogen alpha chain × 1 (P02671) Fibrinogen, gamma polypeptide × 1 (Q53Y18) Gly-hydroxyPro-Arg-Pro-amide peptide ligand × 2 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 7.5;295 K;equal volumes of 10 mg/ml fragment D, 5 mM Gly-hydroxyPro-Arg-Pro-amide, 50 mM Tris, pH 7.0 and 16% PEG 3350, 50 mM Tris pH 8.0 mM 20 mM CaCl2, 2 mM sodium azide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.90 Å R-free 0.347

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 54 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 Author chain H; PDBConstruct 1–328; UniProt 164–491 Author chain K; PDBConstruct 1–328; UniProt 164–491

Fibrinogen, gamma polypeptide

OrganismNot specified

UniProt Q53Y18

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 115–437 Not recorded Fibrinogen alpha chain × 1 (P02671) Fibrinogen beta chain × 1 (P02675) Gly-hydroxyPro-Arg-Pro-amide peptide ligand × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;equal volumes of 10 mg/ml fragment D, 5 mM Gly-hydroxyPro-Arg-Pro-amide, 50 mM Tris, pH 7.0 and 16% PEG 3350, 50 mM Tris pH 8.0 mM 20 mM CaCl2, 2 mM sodium azide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.90 Å R-free 0.347
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain F; UniProt 115–437 Not recorded Fibrinogen alpha chain × 1 (P02671) Fibrinogen beta chain × 1 (P02675) Gly-hydroxyPro-Arg-Pro-amide peptide ligand × 2 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 7.5;295 K;equal volumes of 10 mg/ml fragment D, 5 mM Gly-hydroxyPro-Arg-Pro-amide, 50 mM Tris, pH 7.0 and 16% PEG 3350, 50 mM Tris pH 8.0 mM 20 mM CaCl2, 2 mM sodium azide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.90 Å R-free 0.347
3 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain I; UniProt 115–437 Not recorded Fibrinogen alpha chain × 1 (P02671) Fibrinogen beta chain × 1 (P02675) Gly-hydroxyPro-Arg-Pro-amide peptide ligand × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;equal volumes of 10 mg/ml fragment D, 5 mM Gly-hydroxyPro-Arg-Pro-amide, 50 mM Tris, pH 7.0 and 16% PEG 3350, 50 mM Tris pH 8.0 mM 20 mM CaCl2, 2 mM sodium azide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.90 Å R-free 0.347
4 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain L; UniProt 115–437 Not recorded Fibrinogen alpha chain × 1 (P02671) Fibrinogen beta chain × 1 (P02675) Gly-hydroxyPro-Arg-Pro-amide peptide ligand × 2 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 7.5;295 K;equal volumes of 10 mg/ml fragment D, 5 mM Gly-hydroxyPro-Arg-Pro-amide, 50 mM Tris, pH 7.0 and 16% PEG 3350, 50 mM Tris pH 8.0 mM 20 mM CaCl2, 2 mM sodium azide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.90 Å R-free 0.347

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.

7 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q53Y18_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–323; UniProt 115–437 Author chain F; PDBConstruct 1–323; UniProt 115–437 Author chain I; PDBConstruct 1–323; UniProt 115–437 Author chain L; PDBConstruct 1–323; UniProt 115–437

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 2hod

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2hod
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2hod
Deposition date deposition_date2006-07-14
Structure title titleCrystal Structure of Fragment D from Human Fibrinogen Complexed with Gly-hydroxyPro-Arg-Pro-amide
Keywords keywordsKnob-hole interactions, BLOOD CLOTTING-PEPTIDE complex; BLOOD CLOTTING/PEPTIDE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier70.08
Radius of gyration Rg (electron density) rg_electron71.67
Forward intensity I(0) i01526480000.00
Molecular weight molecular_weight317180.0 kDa
Excluded volume excluded_volume391970 ų
Envelope volume envelope_volume586980 ų
Hydration-shell volume shell_volume77142 ų
Envelope diameter envelope_diameter306.6
Shell Rg shell_rg57.27
Envelope Rg envelope_rg73.49
Shape Rg shape_rg71.57
Total Rg total_rg71.71
Total atoms total_atoms22278
Residues n_residues2754
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 dmax219.0
Rg (real space) rg_real68.71
Rg uncertainty (real space) rg_real_error1.96
I(0) (real space) i0_real1.5120e+09
I(0) uncertainty (real space) i0_real_error3.0670e+07
Rg (reciprocal space) rg_reciprocal67.18
I(0) (reciprocal space) i0_reciprocal1516000000.0000
Solution quality estimate total_estimate0.8381
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary59.7
Skewness Skewness skewness0.600
Kurtosis Kurtosis kurtosis-0.256
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0243
Highest regularization parameter α highest_alpha32490000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.847; Stabil: 0.990; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.361

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 28 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2hoda1
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_idd2hodd1
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_idd2hodg1
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_idd2hodj1
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 (24 domains)

Domain ID domain_id2hodA00
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_id2hodB01
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_id2hodB02
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_id2hodB03
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_id2hodC01
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_id2hodC02
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_id2hodD00
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_id2hodE01
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_id2hodE02
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_id2hodE03
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_id2hodF01
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_id2hodF02
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_id2hodG00
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_id2hodH01
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_id2hodH02
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_id2hodH03
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_id2hodI01
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_id2hodI02
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_id2hodJ00
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_id2hodK01
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_id2hodK02
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_id2hodK03
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_id2hodL01
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_id2hodL02
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

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9. Files and Curves (10)