4duu

The X-ray Crystal Structure of Full-Length type I Human Plasminogen

Method: X-RAY DIFFRACTION Dmax: 104.7 Å Quality: GOOD

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

Plasminogen

OrganismNot specified

UniProt P00747

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 20–810 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.4;293 K;2M sodium formate, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 5.20 Å R-free 0.312

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.

46 other PDB entries and 76 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PLMN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–791; UniProt 20–810

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 4duu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4duu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4duu
Deposition date deposition_date2012-02-22
Structure title titleThe X-ray Crystal Structure of Full-Length type I Human Plasminogen
Keywords keywordsserine protease, fibrinolysis, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.55
Radius of gyration Rg (electron density) rg_electron30.00
Forward intensity I(0) i0100769000.00
Molecular weight molecular_weight75267.0 kDa
Excluded volume excluded_volume92405 ų
Envelope volume envelope_volume125320 ų
Hydration-shell volume shell_volume35461 ų
Envelope diameter envelope_diameter109.3
Shell Rg shell_rg36.54
Envelope Rg envelope_rg29.67
Shape Rg shape_rg30.01
Total Rg total_rg30.53
Total atoms total_atoms5272
Residues n_residues682
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 dmax104.7
Rg (real space) rg_real30.54
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real1.0080e+08
I(0) uncertainty (real space) i0_real_error1.5200e+06
Rg (reciprocal space) rg_reciprocal30.55
I(0) (reciprocal space) i0_reciprocal100800000.0000
Solution quality estimate total_estimate0.8807
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.2
Skewness Skewness skewness0.323
Kurtosis Kurtosis kurtosis-0.265
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11880000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.841; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.969; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)