1tfx

COMPLEX OF THE SECOND KUNITZ DOMAIN OF TISSUE FACTOR PATHWAY INHIBITOR WITH PORCINE TRYPSIN

Method: X-RAY DIFFRACTION Dmax: 109.7 Å Quality: GOOD

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

TRYPSIN

Sus scrofa

UniProt P00761

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 9–231 Not recorded TISSUE FACTOR PATHWAY INHIBITOR × 1 (P10646) CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 2.60 Å
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 9–231 Not recorded TISSUE FACTOR PATHWAY INHIBITOR × 1 (P10646) CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 2.60 Å

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.

44 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRYP_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–223; UniProt 9–231 Author chain B; PDBConstruct 1–223; UniProt 9–231

TISSUE FACTOR PATHWAY INHIBITOR

Homo sapiens

UniProt P10646

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 121–178 Fragment:FACTOR XA-BINDING DOMAIN, DOMAIN II TRYPSIN × 1 (P00761) CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 2.60 Å
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 121–178 Fragment:FACTOR XA-BINDING DOMAIN, DOMAIN II TRYPSIN × 1 (P00761) CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;pH 8.0 Resolution 2.60 Å

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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TFPI1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–58; UniProt 121–178 Author chain D; PDBConstruct 1–58; UniProt 121–178

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 1tfx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1tfx
Deposition date deposition_date1997-01-21
Structure title titleCOMPLEX OF THE SECOND KUNITZ DOMAIN OF TISSUE FACTOR PATHWAY INHIBITOR WITH PORCINE TRYPSIN
Keywords keywordsCOMPLEX (SERINE PROTEASE-INHIBITOR), HYDROLASE, INHIBITOR, BLOOD COAGULATION, COMPLEX (SERINE PROTEASE-INHIBITOR) complex; COMPLEX (SERINE PROTEASE/INHIBITOR)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.36
Radius of gyration Rg (electron density) rg_electron32.32
Forward intensity I(0) i063676500.00
Molecular weight molecular_weight60725.0 kDa
Excluded volume excluded_volume74780 ų
Envelope volume envelope_volume95510 ų
Hydration-shell volume shell_volume25927 ų
Envelope diameter envelope_diameter111.3
Shell Rg shell_rg37.25
Envelope Rg envelope_rg31.86
Shape Rg shape_rg32.31
Total Rg total_rg32.74
Total atoms total_atoms4240
Residues n_residues556
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 dmax109.7
Rg (real space) rg_real32.70
Rg uncertainty (real space) rg_real_error1.17
I(0) (real space) i0_real6.3680e+07
I(0) uncertainty (real space) i0_real_error9.7690e+05
Rg (reciprocal space) rg_reciprocal32.56
I(0) (reciprocal space) i0_reciprocal63670000.0000
Solution quality estimate total_estimate0.8077
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.6
Skewness Skewness skewness0.424
Kurtosis Kurtosis kurtosis-0.660
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8398000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.687; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.581; Smooth: 0.860

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1tfxa_
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_idd1tfxb_
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_idd1tfxc_
Class classg — Small proteins
Fold Fold foldg.8 — BPTI-like
Superfamily Superfamily superfamilyg.8.1 — BPTI-like
Family Family familyg.8.1.1 — Small Kunitz-type inhibitors & BPTI-like toxins
Domain ID domain_idd1tfxd_
Class classg — Small proteins
Fold Fold foldg.8 — BPTI-like
Superfamily Superfamily superfamilyg.8.1 — BPTI-like
Family Family familyg.8.1.1 — Small Kunitz-type inhibitors & BPTI-like toxins

CATH v4.4 (6 domains)

Domain ID domain_id1tfxA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1tfxA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1tfxB01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1tfxB02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id1tfxC00
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology410 — Factor Xa Inhibitor
Homologous superfamily homologous superfamily10 — Pancreatic trypsin inhibitor Kunitz domain
Domain ID domain_id1tfxD00
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology410 — Factor Xa Inhibitor
Homologous superfamily homologous superfamily10 — Pancreatic trypsin inhibitor Kunitz domain

8. Citations (7)

9. Files and Curves (10)