1hpk

SOLUTION NMR STRUCTURE OF THE HUMAN PLASMINOGEN KRINGLE 1 DOMAIN COMPLEXED WITH 6-AMINOHEXANOIC ACID AT PH 5.3, 310K, DERIVED FROM RANDOMLY GENERATED STRUCTURES USING SIMULATED ANNEALING, MINIMIZED AVERAGE STRUCTURE

Method: SOLUTION NMR Dmax: 43.3 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 103–181 Fragment:KRINGLE 1 DOMAIN ACA 6-AMINOHEXANOIC ACID × 1 SOLUTION NMR NMR measurement conditions:pH 5.3;310 K 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 1–79; UniProt 103–181

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 1hpk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1hpk
Deposition date deposition_date1996-08-14
Structure title titleSOLUTION NMR STRUCTURE OF THE HUMAN PLASMINOGEN KRINGLE 1 DOMAIN COMPLEXED WITH 6-AMINOHEXANOIC ACID AT PH 5.3, 310K, DERIVED FROM RANDOMLY GENERATED STRUCTURES USING SIMULATED ANNEALING, MINIMIZED AVERAGE STRUCTURE
Keywords keywordsSERINE PROTEASE, FIBRINOLYTIC ENZYME, LYSINE-BINDING DOMAIN; SERINE PROTEASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier12.73
Radius of gyration Rg (electron density) rg_electron11.58
Forward intensity I(0) i02162570.00
Molecular weight molecular_weight9196.0 kDa
Excluded volume excluded_volume11097 ų
Envelope volume envelope_volume12042 ų
Hydration-shell volume shell_volume9003 ų
Envelope diameter envelope_diameter41.4
Shell Rg shell_rg17.05
Envelope Rg envelope_rg12.04
Shape Rg shape_rg11.54
Total Rg total_rg12.91
Total atoms total_atoms1232
Residues n_residues79
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 dmax43.3
Rg (real space) rg_real12.68
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real2.1630e+06
I(0) uncertainty (real space) i0_real_error2.7570e+04
Rg (reciprocal space) rg_reciprocal12.68
I(0) (reciprocal space) i0_reciprocal2163000.0000
Solution quality estimate total_estimate0.8697
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.9
Skewness Skewness skewness0.243
Kurtosis Kurtosis kurtosis-0.243
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha407100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.776; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.980

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1hpka_
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_id1hpkA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology20 — Plasminogen Kringle 4
Homologous superfamily homologous superfamily10 — Plasminogen Kringle 4

8. Citations (2)

9. Files and Curves (10)