1ycp

THE CRYSTAL STRUCTURE OF FIBRINOGEN-AA PEPTIDE 1-23 (F8Y) BOUND TO BOVINE THROMBIN EXPLAINS WHY THE MUTATION OF PHE-8 TO TYROSINE STRONGLY INHIBITS NORMAL CLEAVAGE AT ARGININE-16

Method: X-RAY DIFFRACTION Dmax: 90.1 Å Quality: GOOD

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

EPSILON THROMBIN

OrganismNot specified

UniProt P00735

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 H; UniProt 367–625 Chain L; UniProt 318–366 Not recorded FIBRINOPEPTIDE A-ALPHA × 1 (P02671) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;2.0M AMMONIUM SULFATE 0.1M HEPES, PH 7.5 2.0% POLYETHYLENE GLYCOL 400 Resolution 2.50 Å R-free 0.245
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain J; UniProt 318–366 Chain K; UniProt 367–516 Chain M; UniProt 517–625 Not recorded FIBRINOPEPTIDE A-ALPHA × 1 (P02671) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;2.0M AMMONIUM SULFATE 0.1M HEPES, PH 7.5 2.0% POLYETHYLENE GLYCOL 400 Resolution 2.50 Å R-free 0.245

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 THRB_BOVIN
Isoform
PDB entities 1, 2, 4, 5
Chains and sequence ranges Author chain J; PDBConstruct 1–49; UniProt 318–366 Author chain L; PDBConstruct 1–49; UniProt 318–366 Author chain H; PDBConstruct 1–259; UniProt 367–625 Author chain K; PDBConstruct 1–150; UniProt 367–516 Author chain M; PDBConstruct 1–109; UniProt 517–625

FIBRINOPEPTIDE A-ALPHA

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 20–42 Fragment:RESIDUES 1 - 23 Mutation:F308Y EPSILON THROMBIN × 1 (P00735) ALPHA THROMBIN × 1 (P00735) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;2.0M AMMONIUM SULFATE 0.1M HEPES, PH 7.5 2.0% POLYETHYLENE GLYCOL 400 Resolution 2.50 Å R-free 0.245
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain N; UniProt 20–42 Fragment:RESIDUES 1 - 23 Mutation:F308Y EPSILON THROMBIN × 1 (P00735) EPSILON THROMBIN × 1 (P00735) EPSILON THROMBIN × 1 (P00735) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;2.0M AMMONIUM SULFATE 0.1M HEPES, PH 7.5 2.0% POLYETHYLENE GLYCOL 400 Resolution 2.50 Å R-free 0.245

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 3
Chains and sequence ranges Author chain F; PDBConstruct 1–23; UniProt 20–42 Author chain N; PDBConstruct 1–23; UniProt 20–42

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 1ycp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ycp
Deposition date deposition_date1997-05-01
Structure title titleTHE CRYSTAL STRUCTURE OF FIBRINOGEN-AA PEPTIDE 1-23 (F8Y) BOUND TO BOVINE THROMBIN EXPLAINS WHY THE MUTATION OF PHE-8 TO TYROSINE STRONGLY INHIBITS NORMAL CLEAVAGE AT ARGININE-16
Keywords keywordsFIBRINOPEPTIDE-A, COMPLEX (SERINE PROTEASE-PEPTIDE), THROMBIN, HYDROLASE-HYDROLASE SUBSTRATE COMPLEX; HYDROLASE/HYDROLASE SUBSTRATE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.48
Radius of gyration Rg (electron density) rg_electron28.34
Forward intensity I(0) i067160500.00
Molecular weight molecular_weight64890.0 kDa
Excluded volume excluded_volume81600 ų
Envelope volume envelope_volume99806 ų
Hydration-shell volume shell_volume29442 ų
Envelope diameter envelope_diameter94.5
Shell Rg shell_rg35.37
Envelope Rg envelope_rg28.13
Shape Rg shape_rg28.34
Total Rg total_rg29.06
Total atoms total_atoms4570
Residues n_residues488
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 dmax90.1
Rg (real space) rg_real29.54
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real6.7160e+07
I(0) uncertainty (real space) i0_real_error1.1350e+06
Rg (reciprocal space) rg_reciprocal29.52
I(0) (reciprocal space) i0_reciprocal67160000.0000
Solution quality estimate total_estimate0.8782
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.7
Skewness Skewness skewness0.292
Kurtosis Kurtosis kurtosis-0.791
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha52490000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.934; Smooth: 0.869

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1ycp.1
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.2 — Eukaryotic proteases
Domain ID domain_idd1ycp.2
Class classb — All beta proteins
Fold Fold foldb.47 — Trypsin-like serine proteases
Superfamily Superfamily superfamilyb.47.1 — Trypsin-like serine proteases
Family Family familyb.47.1.2 — Eukaryotic proteases

CATH v4.4 (4 domains)

Domain ID domain_id1ycpH01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1ycpH02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1ycpK00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1ycpM00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases

8. Citations (2)

9. Files and Curves (10)