8crb

Cryo-EM structure of PcrV/Fab(11-E5)

Method: ELECTRON MICROSCOPY Dmax: 109.2 Å Quality: GOOD

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

Maltose/maltodextrin-binding periplasmic protein,Type III secretion protein PcrV

Pseudomonas aeruginosa

UniProt G3XD49

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 2–294 Not recorded Heavy chain × 1 Light chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;1xPBS cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 4.60 Å

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.

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

View Construct and Data Evidence
UniProt name G3XD49_PSEAE
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 400–692; UniProt 2–294

Maltose/maltodextrin-binding periplasmic protein,Type III secretion protein PcrV

Pseudomonas aeruginosa

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 29–384 Not recorded Heavy chain × 1 Light chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;1xPBS cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 4.60 Å

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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 44–399; UniProt 29–384

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 8crb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8crb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8crb
Deposition date deposition_date2023-03-08
最后修订 last_revision2023-11-22
Structure title titleCryo-EM structure of PcrV/Fab(11-E5)
Keywords keywordsantibody T3SS Tip protein, ANTIMICROBIAL PROTEIN; ANTIMICROBIAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier31.41
Radius of gyration Rg (electron density) rg_electron31.32
Forward intensity I(0) i064629800.00
Molecular weight molecular_weight62181.0 kDa
Excluded volume excluded_volume77393 ų
Envelope volume envelope_volume107240 ų
Hydration-shell volume shell_volume30800 ų
Envelope diameter envelope_diameter115.4
Shell Rg shell_rg35.65
Envelope Rg envelope_rg30.91
Shape Rg shape_rg31.29
Total Rg total_rg31.80
Total atoms total_atoms8665
Residues n_residues582
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 dmax109.2
Rg (real space) rg_real31.66
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real6.4630e+07
I(0) uncertainty (real space) i0_real_error1.2610e+06
Rg (reciprocal space) rg_reciprocal31.56
I(0) (reciprocal space) i0_reciprocal64620000.0000
Solution quality estimate total_estimate0.8545
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.8
Skewness Skewness skewness0.533
Kurtosis Kurtosis kurtosis-0.194
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11090000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.784; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.885; Smooth: 0.869

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)