2q9i

Crystal Structure of D-Dimer from Human Fibrin Complexed with Met-His-Arg-Pro-Tyr-amide.

Method: X-RAY DIFFRACTION Dmax: 207.4 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 × 5 其他Polymer 1 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 130–216 Fragment:UNP residues 130-216 Fibrinogen beta chain × 1 (P02675) Fibrinogen, gamma polypeptide × 1 (Q53Y18) Fibrin B Knob (GHRPam) × 1 Fibrin B Knob (MHRPYam) × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;equal volumes of (a) 9 mg/ml D-dimer, 2 mM Gly-His-Arg-Pro-amide, 0.05 M Tris, pH 7.0, 5 mM CaCl2 and (b) 10% PEG, 5 mM CaCl2, 0.05M Tris, pH 8.0, 2 mM sodium azide. Crystals were subsequently soaked in same solution containing 0.6 mM Met-His-Arg-Pro-Tyr-amide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295.0K Resolution 2.80 Å R-free 0.276
2 Other combination Heteromer Protein × 5 其他Polymer 1 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 130–216 Fragment:UNP residues 130-216 Fibrinogen beta chain × 1 (P02675) Fibrinogen, gamma polypeptide × 1 (Q53Y18) Fibrin B Knob (GHRPam) × 1 Fibrin B Knob (MHRPYam) × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;equal volumes of (a) 9 mg/ml D-dimer, 2 mM Gly-His-Arg-Pro-amide, 0.05 M Tris, pH 7.0, 5 mM CaCl2 and (b) 10% PEG, 5 mM CaCl2, 0.05M Tris, pH 8.0, 2 mM sodium azide. Crystals were subsequently soaked in same solution containing 0.6 mM Met-His-Arg-Pro-Tyr-amide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295.0K Resolution 2.80 Å R-free 0.276

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 × 5 其他Polymer 1 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 164–491 Fragment:UNP residues 164-491 Fibrinogen alpha chain × 1 (P02671) Fibrinogen, gamma polypeptide × 1 (Q53Y18) Fibrin B Knob (GHRPam) × 1 Fibrin B Knob (MHRPYam) × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;equal volumes of (a) 9 mg/ml D-dimer, 2 mM Gly-His-Arg-Pro-amide, 0.05 M Tris, pH 7.0, 5 mM CaCl2 and (b) 10% PEG, 5 mM CaCl2, 0.05M Tris, pH 8.0, 2 mM sodium azide. Crystals were subsequently soaked in same solution containing 0.6 mM Met-His-Arg-Pro-Tyr-amide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295.0K Resolution 2.80 Å R-free 0.276
2 Other combination Heteromer Protein × 5 其他Polymer 1 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 164–491 Fragment:UNP residues 164-491 Fibrinogen alpha chain × 1 (P02671) Fibrinogen, gamma polypeptide × 1 (Q53Y18) Fibrin B Knob (GHRPam) × 1 Fibrin B Knob (MHRPYam) × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;equal volumes of (a) 9 mg/ml D-dimer, 2 mM Gly-His-Arg-Pro-amide, 0.05 M Tris, pH 7.0, 5 mM CaCl2 and (b) 10% PEG, 5 mM CaCl2, 0.05M Tris, pH 8.0, 2 mM sodium azide. Crystals were subsequently soaked in same solution containing 0.6 mM Met-His-Arg-Pro-Tyr-amide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295.0K Resolution 2.80 Å R-free 0.276

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 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 Other combination Heteromer Protein × 5 其他Polymer 1 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 114–437 Fragment:UNP residues 114-437 Fibrinogen alpha chain × 1 (P02671) Fibrinogen beta chain × 1 (P02675) Fibrin B Knob (GHRPam) × 1 Fibrin B Knob (MHRPYam) × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;equal volumes of (a) 9 mg/ml D-dimer, 2 mM Gly-His-Arg-Pro-amide, 0.05 M Tris, pH 7.0, 5 mM CaCl2 and (b) 10% PEG, 5 mM CaCl2, 0.05M Tris, pH 8.0, 2 mM sodium azide. Crystals were subsequently soaked in same solution containing 0.6 mM Met-His-Arg-Pro-Tyr-amide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295.0K Resolution 2.80 Å R-free 0.276
2 Other combination Heteromer Protein × 5 其他Polymer 1 PDB declaration: pentameric(5) Consistent with protein copy count Chain F; UniProt 114–437 Fragment:UNP residues 114-437 Fibrinogen alpha chain × 1 (P02671) Fibrinogen beta chain × 1 (P02675) Fibrin B Knob (GHRPam) × 1 Fibrin B Knob (MHRPYam) × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;equal volumes of (a) 9 mg/ml D-dimer, 2 mM Gly-His-Arg-Pro-amide, 0.05 M Tris, pH 7.0, 5 mM CaCl2 and (b) 10% PEG, 5 mM CaCl2, 0.05M Tris, pH 8.0, 2 mM sodium azide. Crystals were subsequently soaked in same solution containing 0.6 mM Met-His-Arg-Pro-Tyr-amide., pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 295.0K Resolution 2.80 Å R-free 0.276

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 15 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 1–324; UniProt 114–437 Author chain F; PDBConstruct 1–324; UniProt 114–437

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 2q9i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2q9i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2q9i
Deposition date deposition_date2007-06-12
Structure title titleCrystal Structure of D-Dimer from Human Fibrin Complexed with Met-His-Arg-Pro-Tyr-amide.
Keywords keywords;fibrin clots, B-knobs, beta-holes, Blood coagulation, Disease mutation, Glycoprotein, Phosphoprotein, Secreted, Pyrrolidone carboxylic acid, 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_guinier53.83
Radius of gyration Rg (electron density) rg_electron55.35
Forward intensity I(0) i0363194000.00
Molecular weight molecular_weight151700.0 kDa
Excluded volume excluded_volume187220 ų
Envelope volume envelope_volume246790 ų
Hydration-shell volume shell_volume44767 ų
Envelope diameter envelope_diameter222.5
Shell Rg shell_rg43.52
Envelope Rg envelope_rg56.97
Shape Rg shape_rg55.23
Total Rg total_rg55.31
Total atoms total_atoms10651
Residues n_residues1315
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 dmax207.4
Rg (real space) rg_real54.91
Rg uncertainty (real space) rg_real_error3.17
I(0) (real space) i0_real3.6320e+08
I(0) uncertainty (real space) i0_real_error8.3370e+06
Rg (reciprocal space) rg_reciprocal52.93
I(0) (reciprocal space) i0_reciprocal362200000.0000
Solution quality estimate total_estimate0.6457
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.8
Skewness Skewness skewness0.714
Kurtosis Kurtosis kurtosis-0.211
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11150000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.197; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.134; Smooth: 0.666

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id2q9iA00
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_id2q9iB01
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_id2q9iB02
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_id2q9iC01
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_id2q9iC02
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_id2q9iD00
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_id2q9iE01
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_id2q9iE02
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_id2q9iF01
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_id2q9iF02
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)