8cpl

YZw2 a scaffold for cryo-EM of small proteins of interest

Method: X-RAY DIFFRACTION Dmax: 125.6 Å Quality: EXCELLENT

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

Putrescine aminotransferase,Immunoglobulin G-binding protein A

Staphylococcus aureus

UniProt P38507

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 Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 220–269 Chain B; UniProt 220–269 Chain C; UniProt 220–269 Chain D; UniProt 220–269 Not recorded PLP PYRIDOXAL-5'-PHOSPHATE × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;16.6% w/v PEG3350, 0.2M NaF and 0.1M Bis-Tris Propane pH 5.5 Resolution 1.60 Å R-free 0.210

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.

66 other PDB entries and 127 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPA_STAAU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 452–501; UniProt 220–269 Author chain B; PDBConstruct 452–501; UniProt 220–269 Author chain C; PDBConstruct 452–501; UniProt 220–269 Author chain D; PDBConstruct 452–501; UniProt 220–269

Putrescine aminotransferase,Immunoglobulin G-binding protein A

Staphylococcus aureus

UniProt P42588

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 Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 7–457 Chain B; UniProt 7–457 Chain C; UniProt 7–457 Chain D; UniProt 7–457 Not recorded PLP PYRIDOXAL-5'-PHOSPHATE × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;16.6% w/v PEG3350, 0.2M NaF and 0.1M Bis-Tris Propane pH 5.5 Resolution 1.60 Å R-free 0.210

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.

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

View Construct and Data Evidence
UniProt name PAT_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–451; UniProt 7–457 Author chain B; PDBConstruct 1–451; UniProt 7–457 Author chain C; PDBConstruct 1–451; UniProt 7–457 Author chain D; PDBConstruct 1–451; UniProt 7–457

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 8cpl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8cpl
Deposition date deposition_date2023-03-03
最后修订 last_revision2024-06-12
Structure title titleYZw2 a scaffold for cryo-EM of small proteins of interest
Keywords keywordsScaffold Fusion protein, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier40.20
Radius of gyration Rg (electron density) rg_electron39.50
Forward intensity I(0) i0597256000.00
Molecular weight molecular_weight202620.0 kDa
Excluded volume excluded_volume254490 ų
Envelope volume envelope_volume315490 ų
Hydration-shell volume shell_volume64731 ų
Envelope diameter envelope_diameter140.5
Shell Rg shell_rg46.56
Envelope Rg envelope_rg39.74
Shape Rg shape_rg39.49
Total Rg total_rg39.89
Total atoms total_atoms14223
Residues n_residues1863
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 dmax125.6
Rg (real space) rg_real40.13
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real5.9730e+08
I(0) uncertainty (real space) i0_real_error9.4260e+06
Rg (reciprocal space) rg_reciprocal40.20
I(0) (reciprocal space) i0_reciprocal597300000.0000
Solution quality estimate total_estimate0.9035
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.9
Skewness Skewness skewness0.206
Kurtosis Kurtosis kurtosis-0.742
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha148700000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.947

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)