1hpj

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, 12 STRUCTURES

Method: SOLUTION NMR Dmax: 38.3 Å Quality: REASONABLE

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 No other associated polymer 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 1hpj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1hpj
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, 12 STRUCTURES
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_guinier11.58
Radius of gyration Rg (electron density) rg_electron11.52
Forward intensity I(0) i0207347000.00
Molecular weight molecular_weight108780.0 kDa
Excluded volume excluded_volume130950 ų
Envelope volume envelope_volume16443 ų
Hydration-shell volume shell_volume10943 ų
Envelope diameter envelope_diameter43.1
Shell Rg shell_rg18.54
Envelope Rg envelope_rg13.12
Shape Rg shape_rg11.47
Total Rg total_rg11.85
Total atoms total_atoms14520
Residues n_residues948
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 dmax38.3
Rg (real space) rg_real11.53
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real2.0730e+08
I(0) uncertainty (real space) i0_real_error2.0800e+06
Rg (reciprocal space) rg_reciprocal11.53
I(0) (reciprocal space) i0_reciprocal207300000.0000
Solution quality estimate total_estimate0.6639
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.6
Skewness Skewness skewness0.209
Kurtosis Kurtosis kurtosis-0.308
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha139600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.842; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 0.997; 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_idd1hpja_
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_id1hpjA00
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)