4dcb

Y. pestis Plasminogen Activator Pla in Complex with Human Plasminogen Activation Loop Peptide ALP11

Method: X-RAY DIFFRACTION Dmax: 78.7 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Coagulase/fibrinolysin

Yersinia pestis

UniProt P17811

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 25–312 Mutation:D84N Plasminogen × 1 (P00747) MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 4 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 C8E (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE × 1 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;45% (v/v) 2-methyl-2,4-pentanediol (MPD), 0.2 M NH4KH2PO4 and 0.1M NaOAc, pH 5.5, VAPOR DIFFUSION, HANGING DROP Resolution 2.03 Å R-free 0.232

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.

3 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COLY_YERPE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–288; UniProt 25–312

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 576–585 Not recorded Coagulase/fibrinolysin × 1 (P17811) MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 4 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 C8E (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE × 1 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;45% (v/v) 2-methyl-2,4-pentanediol (MPD), 0.2 M NH4KH2PO4 and 0.1M NaOAc, pH 5.5, VAPOR DIFFUSION, HANGING DROP Resolution 2.03 Å R-free 0.232

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 2
Chains and sequence ranges Author chain F; PDBConstruct 1–10; UniProt 576–585

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 4dcb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4dcb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4dcb
Deposition date deposition_date2012-01-17
Structure title titleY. pestis Plasminogen Activator Pla in Complex with Human Plasminogen Activation Loop Peptide ALP11
Keywords keywordsBeta barrel, Plasminogen activator, Protease, Outer membrane, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.83
Radius of gyration Rg (electron density) rg_electron22.53
Forward intensity I(0) i019636700.00
Molecular weight molecular_weight33164.0 kDa
Excluded volume excluded_volume41245 ų
Envelope volume envelope_volume49313 ų
Hydration-shell volume shell_volume19449 ų
Envelope diameter envelope_diameter79.8
Shell Rg shell_rg28.16
Envelope Rg envelope_rg23.00
Shape Rg shape_rg22.51
Total Rg total_rg23.34
Total atoms total_atoms2341
Residues n_residues288
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 dmax78.7
Rg (real space) rg_real23.04
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real1.9640e+07
I(0) uncertainty (real space) i0_real_error2.6320e+05
Rg (reciprocal space) rg_reciprocal22.99
I(0) (reciprocal space) i0_reciprocal19640000.0000
Solution quality estimate total_estimate0.8295
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.5
Skewness Skewness skewness0.566
Kurtosis Kurtosis kurtosis-0.293
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5737000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.681; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.755; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)