1tpk

CRYSTAL STRUCTURE OF THE KRINGLE-2 DOMAIN OF TISSUE PLASMINOGEN ACTIVATOR AT 2.4-ANGSTROMS RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 76.0 Å Quality: GOOD

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

TISSUE 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 211–298 Not recorded CL CHLORIDE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.40 Å
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 211–298 Not recorded CL CHLORIDE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.40 Å
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 211–298 Not recorded CL CHLORIDE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.40 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.

10 other PDB entries and 14 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 1–88; UniProt 211–298 Author chain B; PDBConstruct 1–88; UniProt 211–298 Author chain C; PDBConstruct 1–88; UniProt 211–298

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 1tpk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1tpk
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1tpk
Deposition date deposition_date1991-09-24
Structure title titleCRYSTAL STRUCTURE OF THE KRINGLE-2 DOMAIN OF TISSUE PLASMINOGEN ACTIVATOR AT 2.4-ANGSTROMS RESOLUTION
Keywords keywordsPLASMINOGEN ACTIVATOR; PLASMINOGEN ACTIVATOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.42
Radius of gyration Rg (electron density) rg_electron21.60
Forward intensity I(0) i017130300.00
Molecular weight molecular_weight29041.0 kDa
Excluded volume excluded_volume35308 ų
Envelope volume envelope_volume44186 ų
Hydration-shell volume shell_volume18092 ų
Envelope diameter envelope_diameter78.8
Shell Rg shell_rg26.84
Envelope Rg envelope_rg21.69
Shape Rg shape_rg21.58
Total Rg total_rg22.34
Total atoms total_atoms2028
Residues n_residues255
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 dmax76.0
Rg (real space) rg_real22.46
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real1.7130e+07
I(0) uncertainty (real space) i0_real_error2.2460e+05
Rg (reciprocal space) rg_reciprocal22.45
I(0) (reciprocal space) i0_reciprocal17130000.0000
Solution quality estimate total_estimate0.8828
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.7
Skewness Skewness skewness0.302
Kurtosis Kurtosis kurtosis-0.547
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3772000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.886; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1tpka_
Class classg — Small proteins
Fold Fold foldg.14 — Kringle-like
Superfamily Superfamily superfamilyg.14.1 — Kringle-like
Family Family familyg.14.1.1 — Kringle modules
Domain ID domain_idd1tpkb_
Class classg — Small proteins
Fold Fold foldg.14 — Kringle-like
Superfamily Superfamily superfamilyg.14.1 — Kringle-like
Family Family familyg.14.1.1 — Kringle modules
Domain ID domain_idd1tpkc_
Class classg — Small proteins
Fold Fold foldg.14 — Kringle-like
Superfamily Superfamily superfamilyg.14.1 — Kringle-like
Family Family familyg.14.1.1 — Kringle modules

CATH v4.4 (3 domains)

Domain ID domain_id1tpkA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology20 — Plasminogen Kringle 4
Homologous superfamily homologous superfamily10 — Plasminogen Kringle 4
Domain ID domain_id1tpkB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology20 — Plasminogen Kringle 4
Homologous superfamily homologous superfamily10 — Plasminogen Kringle 4
Domain ID domain_id1tpkC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology20 — Plasminogen Kringle 4
Homologous superfamily homologous superfamily10 — Plasminogen Kringle 4

8. Citations (1)

9. Files and Curves (10)