2l0s

Solution Structure of Human Plasminogen Kringle 3

Method: SOLUTION NMR Dmax: 39.1 Å Quality: REASONABLE

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

Plasminogen

Homo sapiens

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 272–354 Fragment:UNP residues 272-354, Kringle 3 Domain Mutation:C43S No other associated polymer SOLUTION NMR NMR measurement conditions:298 K;Ionic strength (raw mmCIF value) 0;Pressure ambient NMR measurement conditions:298 K;Ionic strength (raw mmCIF value) 0;Pressure ambient NMR sample composition:1.0 mM [U-97% 15N] hPgn rK3-1, 90% H2O/10% D2O | 90% H2O/10% D2O 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.

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 1–83; UniProt 272–354

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 2l0s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2l0s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2l0s
Deposition date deposition_date2010-07-15
Structure title titleSolution Structure of Human Plasminogen Kringle 3
Keywords keywordsPlasminogen, Kringle Domain, SERINE PROTEASE, FIBRINOLYSIS, BLOOD CLOTTING; BLOOD CLOTTING
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.95
Radius of gyration Rg (electron density) rg_electron11.88
Forward intensity I(0) i0633895000.00
Molecular weight molecular_weight190270.0 kDa
Excluded volume excluded_volume228240 ų
Envelope volume envelope_volume16496 ų
Hydration-shell volume shell_volume10751 ų
Envelope diameter envelope_diameter44.6
Shell Rg shell_rg18.92
Envelope Rg envelope_rg13.95
Shape Rg shape_rg11.85
Total Rg total_rg12.08
Total atoms total_atoms25500
Residues n_residues1660
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 dmax39.1
Rg (real space) rg_real11.93
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real6.3390e+08
I(0) uncertainty (real space) i0_real_error7.1190e+06
Rg (reciprocal space) rg_reciprocal11.93
I(0) (reciprocal space) i0_reciprocal633900000.0000
Solution quality estimate total_estimate0.6513
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.9
Skewness Skewness skewness0.341
Kurtosis Kurtosis kurtosis-0.141
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha219800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.790; Stabil: 0.998; Sysdev: 0.368; Positv: 1.000; Valcen: 0.996; 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_idd2l0sa_
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 (1 domains)

Domain ID domain_id2l0sA00
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)