1tpn

SOLUTION STRUCTURE OF THE FIBRIN BINDING FINGER DOMAIN OF TISSUE-TYPE PLASMINOGEN ACTIVATOR DETERMINED BY 1H NUCLEAR MAGNETIC RESONANCE

Method: SOLUTION NMR Dmax: 46.8 Å Quality: REASONABLE

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

TISSUE-TYPE PLASMINOGEN ACTIVATOR

Homo sapiens

UniProt P00750

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 36–85 Not recorded No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions Resolution not provided

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.

10 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TPA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–50; UniProt 36–85

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 1tpn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1tpn
Deposition date deposition_date1993-05-26
Structure title titleSOLUTION STRUCTURE OF THE FIBRIN BINDING FINGER DOMAIN OF TISSUE-TYPE PLASMINOGEN ACTIVATOR DETERMINED BY 1H NUCLEAR MAGNETIC RESONANCE
Keywords keywordsPLASMINOGEN ACTIVATOR; PLASMINOGEN ACTIVATOR
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.70
Radius of gyration Rg (electron density) rg_electron12.11
Forward intensity I(0) i0458786000.00
Molecular weight molecular_weight168110.0 kDa
Excluded volume excluded_volume205110 ų
Envelope volume envelope_volume16396 ų
Hydration-shell volume shell_volume9973 ų
Envelope diameter envelope_diameter52.8
Shell Rg shell_rg19.63
Envelope Rg envelope_rg15.65
Shape Rg shape_rg12.08
Total Rg total_rg12.34
Total atoms total_atoms23016
Residues n_residues1400
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 dmax46.8
Rg (real space) rg_real11.85
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real4.5880e+08
I(0) uncertainty (real space) i0_real_error5.3200e+06
Rg (reciprocal space) rg_reciprocal11.84
I(0) (reciprocal space) i0_reciprocal458800000.0000
Solution quality estimate total_estimate0.5030
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary11.8
Skewness Skewness skewness0.628
Kurtosis Kurtosis kurtosis0.164
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha72870.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.496; Stabil: 1.000; Sysdev: 0.256; Positv: 1.000; Valcen: 0.276; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1tpna_
Class classg — Small proteins
Fold Fold foldg.27 — FnI-like domain
Superfamily Superfamily superfamilyg.27.1 — FnI-like domain
Family Family familyg.27.1.1 — Fibronectin type I module

CATH v4.4 (1 domains)

Domain ID domain_id1tpnA00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology70 — Complement Module; domain 1
Homologous superfamily homologous superfamily10 — Complement Module, domain 1

8. Citations (1)

9. Files and Curves (10)