6q1u

Structure of plasmin and peptide complex

Method: X-RAY DIFFRACTION Dmax: 81.7 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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 562–810 Not recorded GLY-ARG-ALA-TYR-LYS-SER-LYS-PRO-PRO-ILE-ALA-PHE-PRO-ASP × 1 WMH 1-methyl-1H-1,2,3-triazole × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;293 K;100 mM Sodium Citrate, 100 mM MgCl2, 18% PEG 4000 Resolution 2.35 Å R-free 0.287
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 562–810 Not recorded GLY-ARG-ALA-TYR-LYS-SER-LYS-PRO-PRO-ILE-ALA-PHE-PRO-ASP × 1 WMH 1-methyl-1H-1,2,3-triazole × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;293 K;100 mM Sodium Citrate, 100 mM MgCl2, 18% PEG 4000 Resolution 2.35 Å R-free 0.287

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 75 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 1–249; UniProt 562–810 Author chain B; PDBConstruct 1–249; UniProt 562–810

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 6q1u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6q1u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6q1u
Deposition date deposition_date2019-08-06
Structure title titleStructure of plasmin and peptide complex
Keywords keywordsserine protease, cyclic peptide, complex, antifibrinolysis, 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_guinier25.14
Radius of gyration Rg (electron density) rg_electron24.55
Forward intensity I(0) i051149600.00
Molecular weight molecular_weight55747.0 kDa
Excluded volume excluded_volume69796 ų
Envelope volume envelope_volume81307 ų
Hydration-shell volume shell_volume27704 ų
Envelope diameter envelope_diameter81.8
Shell Rg shell_rg31.74
Envelope Rg envelope_rg24.62
Shape Rg shape_rg24.56
Total Rg total_rg25.29
Total atoms total_atoms3921
Residues n_residues516
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 dmax81.7
Rg (real space) rg_real25.15
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real5.1150e+07
I(0) uncertainty (real space) i0_real_error7.0810e+05
Rg (reciprocal space) rg_reciprocal25.15
I(0) (reciprocal space) i0_reciprocal51150000.0000
Solution quality estimate total_estimate0.7150
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary27.2
Skewness Skewness skewness0.369
Kurtosis Kurtosis kurtosis-0.407
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha17790000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.874; Stabil: 1.000; Sysdev: 0.242; Positv: 1.000; Valcen: 0.969; Smooth: 0.972

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6q1uA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases
Domain ID domain_id6q1uB02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology10 — Thrombin, subunit H
Homologous superfamily homologous superfamily10 — Trypsin-like serine proteases

8. Citations (1)

9. Files and Curves (10)