2h43

Crystal Structure of Human Fragment D Complexed with Ala-His-Arg-Pro-amide

Method: X-RAY DIFFRACTION Dmax: 219.4 Å Quality: REASONABLE

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 Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 130–216 Not recorded Fibrinogen beta chain × 1 (P02675) Fibrinogen gamma chain × 1 (P02679) GLY-HIS-ARG-PRO-AMIDE peptide ligand × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-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;fragment D, 5 mg/mil, 4mM AHRPam, 50mM Tris, pH 7.5, 7.5% PEG, 7.5mM CaCl2, 1mM sodium azide, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.70 Å R-free 0.307
2 Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 130–216 Not recorded Fibrinogen beta chain × 1 (P02675) Fibrinogen gamma chain × 1 (P02679) GLY-HIS-ARG-PRO-AMIDE peptide ligand × 1 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-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;fragment D, 5 mg/mil, 4mM AHRPam, 50mM Tris, pH 7.5, 7.5% PEG, 7.5mM CaCl2, 1mM sodium azide, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.70 Å R-free 0.307

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 1–87; UniProt 130–216 Author chain D; 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 Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 164–491 Not recorded Fibrinogen alpha chain × 1 (P02671) Fibrinogen gamma chain × 1 (P02679) GLY-HIS-ARG-PRO-AMIDE peptide ligand × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-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;fragment D, 5 mg/mil, 4mM AHRPam, 50mM Tris, pH 7.5, 7.5% PEG, 7.5mM CaCl2, 1mM sodium azide, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.70 Å R-free 0.307
2 Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 164–491 Not recorded Fibrinogen alpha chain × 1 (P02671) Fibrinogen gamma chain × 1 (P02679) GLY-HIS-ARG-PRO-AMIDE peptide ligand × 1 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-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;fragment D, 5 mg/mil, 4mM AHRPam, 50mM Tris, pH 7.5, 7.5% PEG, 7.5mM CaCl2, 1mM sodium azide, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.70 Å R-free 0.307

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

Fibrinogen gamma chain

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 Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 115–433 Not recorded Fibrinogen alpha chain × 1 (P02671) Fibrinogen beta chain × 1 (P02675) GLY-HIS-ARG-PRO-AMIDE peptide ligand × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-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;fragment D, 5 mg/mil, 4mM AHRPam, 50mM Tris, pH 7.5, 7.5% PEG, 7.5mM CaCl2, 1mM sodium azide, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.70 Å R-free 0.307
2 Other combination Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 115–433 Not recorded Fibrinogen alpha chain × 1 (P02671) Fibrinogen beta chain × 1 (P02675) GLY-HIS-ARG-PRO-AMIDE peptide ligand × 1 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-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;fragment D, 5 mg/mil, 4mM AHRPam, 50mM Tris, pH 7.5, 7.5% PEG, 7.5mM CaCl2, 1mM sodium azide, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 2.70 Å R-free 0.307

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 1–319; UniProt 115–433 Author chain F; PDBConstruct 1–319; UniProt 115–433

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 2h43

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2h43
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2h43
Deposition date deposition_date2006-05-23
Structure title titleCrystal Structure of Human Fragment D Complexed with Ala-His-Arg-Pro-amide
Keywords keywordsknob-hole interaction, fragment D, coiled-coil, 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_guinier55.36
Radius of gyration Rg (electron density) rg_electron57.21
Forward intensity I(0) i0369623000.00
Molecular weight molecular_weight153310.0 kDa
Excluded volume excluded_volume189390 ų
Envelope volume envelope_volume252920 ų
Hydration-shell volume shell_volume45042 ų
Envelope diameter envelope_diameter232.5
Shell Rg shell_rg43.77
Envelope Rg envelope_rg58.58
Shape Rg shape_rg57.09
Total Rg total_rg57.13
Total atoms total_atoms10770
Residues n_residues1331
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 dmax219.4
Rg (real space) rg_real56.60
Rg uncertainty (real space) rg_real_error5.55
I(0) (real space) i0_real3.6960e+08
I(0) uncertainty (real space) i0_real_error9.6390e+06
Rg (reciprocal space) rg_reciprocal54.34
I(0) (reciprocal space) i0_reciprocal368400000.0000
Solution quality estimate total_estimate0.6424
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.3
Skewness Skewness skewness0.732
Kurtosis Kurtosis kurtosis-0.152
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10860000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.153; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.065; Smooth: 0.828

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2h43a1
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_idd2h43d1
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_id2h43A00
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_id2h43B01
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_id2h43B02
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_id2h43C01
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_id2h43C02
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_id2h43D00
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_id2h43E01
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_id2h43E02
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_id2h43F01
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_id2h43F02
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)