8r2p

YZwIdeal x16 a scaffold for cryo-EM of small proteins of interest crystallizing in space group 19 (P 21 21 21)

Method: X-RAY DIFFRACTION Dmax: 121.7 Å Quality: EXCELLENT

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

Putrescine aminotransferase,Immunoglobulin G-binding protein A

Escherichia coli

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 218–269 Chain B; UniProt 218–269 Chain C; UniProt 218–269 Chain D; UniProt 218–269 Mutation:G487A PLP PYRIDOXAL-5'-PHOSPHATE × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;50% w/v PEG200, 0.2M MgCl2 and 0.1M Sodium Cacodylate buffer pH 6.5 Resolution 2.22 Å R-free 0.230

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 472–523; UniProt 218–269 Author chain B; PDBConstruct 472–523; UniProt 218–269 Author chain C; PDBConstruct 472–523; UniProt 218–269 Author chain D; PDBConstruct 472–523; UniProt 218–269

Putrescine aminotransferase,Immunoglobulin G-binding protein A

Escherichia coli

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 Mutation:G487A PLP PYRIDOXAL-5'-PHOSPHATE × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;50% w/v PEG200, 0.2M MgCl2 and 0.1M Sodium Cacodylate buffer pH 6.5 Resolution 2.22 Å R-free 0.230

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 14–464; UniProt 7–457 Author chain B; PDBConstruct 14–464; UniProt 7–457 Author chain C; PDBConstruct 14–464; UniProt 7–457 Author chain D; PDBConstruct 14–464; 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 8r2p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8r2p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8r2p
Deposition date deposition_date2023-11-07
最后修订 last_revision2024-11-13
Structure title titleYZwIdeal x16 a scaffold for cryo-EM of small proteins of interest crystallizing in space group 19 (P 21 21 21)
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_guinier39.23
Radius of gyration Rg (electron density) rg_electron38.50
Forward intensity I(0) i0610655000.00
Molecular weight molecular_weight204840.0 kDa
Excluded volume excluded_volume257370 ų
Envelope volume envelope_volume314980 ų
Hydration-shell volume shell_volume65625 ų
Envelope diameter envelope_diameter122.5
Shell Rg shell_rg46.23
Envelope Rg envelope_rg38.54
Shape Rg shape_rg38.47
Total Rg total_rg38.97
Total atoms total_atoms14379
Residues n_residues1884
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 dmax121.7
Rg (real space) rg_real39.11
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real6.1070e+08
I(0) uncertainty (real space) i0_real_error9.5260e+06
Rg (reciprocal space) rg_reciprocal39.19
I(0) (reciprocal space) i0_reciprocal610700000.0000
Solution quality estimate total_estimate0.9070
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.6
Skewness Skewness skewness0.199
Kurtosis Kurtosis kurtosis-0.703
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha161200000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.946; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.949

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)