5hpg

STRUCTURE AND LIGAND DETERMINANTS OF THE RECOMBINANT KRINGLE 5 DOMAIN OF HUMAN PLASMINOGEN

Method: X-RAY DIFFRACTION Dmax: 67.4 Å Quality: GOOD

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 480–563 Chain B; UniProt 480–563 Fragment:KRINGLE 5 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;24% (W/V) PEG 8000, 0.1 M NA-HEPES, PH 7.0, 0.15 M LI2(SO4) Resolution 1.66 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.

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 1–84; UniProt 480–563 Author chain B; PDBConstruct 1–84; UniProt 480–563

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 5hpg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5hpg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5hpg
Deposition date deposition_date1997-09-19
Structure title titleSTRUCTURE AND LIGAND DETERMINANTS OF THE RECOMBINANT KRINGLE 5 DOMAIN OF HUMAN PLASMINOGEN
Keywords keywordsSERINE PROTEASE, KRINGLE 5, HUMAN PLASMINOGEN, FIBRINOLYSIS; SERINE PROTEASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.23
Radius of gyration Rg (electron density) rg_electron17.88
Forward intensity I(0) i07321590.00
Molecular weight molecular_weight18499.0 kDa
Excluded volume excluded_volume22495 ų
Envelope volume envelope_volume26111 ų
Hydration-shell volume shell_volume13229 ų
Envelope diameter envelope_diameter67.2
Shell Rg shell_rg22.76
Envelope Rg envelope_rg18.37
Shape Rg shape_rg17.91
Total Rg total_rg18.57
Total atoms total_atoms1296
Residues n_residues168
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 dmax67.4
Rg (real space) rg_real18.38
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real7.3220e+06
I(0) uncertainty (real space) i0_real_error1.0480e+05
Rg (reciprocal space) rg_reciprocal18.36
I(0) (reciprocal space) i0_reciprocal7322000.0000
Solution quality estimate total_estimate0.7937
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.3
Skewness Skewness skewness0.572
Kurtosis Kurtosis kurtosis-0.176
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1920000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.569; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.620; Smooth: 0.986

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5hpga_
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_idd5hpgb_
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 (2 domains)

Domain ID domain_id5hpgA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology20 — Plasminogen Kringle 4
Homologous superfamily homologous superfamily10 — Plasminogen Kringle 4
Domain ID domain_id5hpgB00
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)