1i5k

STRUCTURE AND BINDING DETERMINANTS OF THE RECOMBINANT KRINGLE-2 DOMAIN OF HUMAN PLASMINOGEN TO AN INTERNAL PEPTIDE FROM A GROUP A STREPTOCOCCAL SURFACE PROTEIN

Method: X-RAY DIFFRACTION Dmax: 67.0 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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 183–262 Chain B; UniProt 183–262 Fragment:MODIFIED RECOMBINANT KRINGLE-2 DOMAIN Mutation:C4G/E56D/L72Y M PROTEIN × 2 (P49054) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;23%(w/v) PEG 3350, 0.1 M Mes, 0.2 M Li2SO4, 2mM CaCl2, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.70 Å R-free 0.262

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 4–84; UniProt 183–262 Author chain B; PDBConstruct 4–84; UniProt 183–262

M PROTEIN

OrganismNot specified

UniProt P49054

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 85–113 Chain D; UniProt 85–113 Fragment:VEK-30 (30 RESIDUE INTERNAL PEPTIDE) PLASMINOGEN × 2 (P00747) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;23%(w/v) PEG 3350, 0.1 M Mes, 0.2 M Li2SO4, 2mM CaCl2, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.70 Å R-free 0.262

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.

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

View Construct and Data Evidence
UniProt name PAM_STRPY
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–30; UniProt 85–113 Author chain D; PDBConstruct 1–30; UniProt 85–113

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 1i5k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1i5k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1i5k
Deposition date deposition_date2001-02-27
Structure title titleSTRUCTURE AND BINDING DETERMINANTS OF THE RECOMBINANT KRINGLE-2 DOMAIN OF HUMAN PLASMINOGEN TO AN INTERNAL PEPTIDE FROM A GROUP A STREPTOCOCCAL SURFACE PROTEIN
Keywords keywordsHuman Plasminogen Kringle-2, Kringles, VEK-30, BLOOD CLOTTING; BLOOD CLOTTING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.85
Radius of gyration Rg (electron density) rg_electron18.11
Forward intensity I(0) i012788700.00
Molecular weight molecular_weight24810.0 kDa
Excluded volume excluded_volume30219 ų
Envelope volume envelope_volume34936 ų
Hydration-shell volume shell_volume16732 ų
Envelope diameter envelope_diameter69.2
Shell Rg shell_rg23.70
Envelope Rg envelope_rg18.41
Shape Rg shape_rg18.00
Total Rg total_rg19.20
Total atoms total_atoms1737
Residues n_residues211
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 dmax67.0
Rg (real space) rg_real18.90
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real1.2790e+07
I(0) uncertainty (real space) i0_real_error1.5400e+05
Rg (reciprocal space) rg_reciprocal18.89
I(0) (reciprocal space) i0_reciprocal12790000.0000
Solution quality estimate total_estimate0.7625
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary20.5
Skewness Skewness skewness0.497
Kurtosis Kurtosis kurtosis-0.018
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3494000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.675; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.887; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1i5ka_
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_idd1i5kb1
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_idd1i5kb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id1i5kA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology20 — Plasminogen Kringle 4
Homologous superfamily homologous superfamily10 — Plasminogen Kringle 4
Domain ID domain_id1i5kB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology20 — Plasminogen Kringle 4
Homologous superfamily homologous superfamily10 — Plasminogen Kringle 4

8. Citations (5)

9. Files and Curves (10)