8uaz

Structure of Glutamyl-5'-O-adenosine phosphoramidate/RNase A

Method: X-RAY DIFFRACTION Dmax: 76.4 Å Quality: GOOD

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

Ribonuclease pancreatic

OrganismNot specified

UniProt P61823

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 27–150 Not recorded WFU (2S)-2-{[(S)-{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl]amino}pentanedioic acid (non-preferred name) × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;PROTEIN WAS CRYSTALLIZED FROM 25 percent PEG 3350, 20 MM SODIUM CITRATE, PH 5.5. Glutaminyl-5'-O-adenosine phosphoramidate soaking was achieved as follows. 1 uL of a stock solution of 100 mM ligand was added to 2uL of reservoir solution, to achieve a concentration of ~35 mM in the soaking solution. A few RNase A crystals were soaked for 110 - 130 minutes in the soaking solution. Resolution 1.76 Å R-free 0.249
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 27–150 Not recorded WFU (2S)-2-{[(S)-{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy}(hydroxy)phosphoryl]amino}pentanedioic acid (non-preferred name) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;PROTEIN WAS CRYSTALLIZED FROM 25 percent PEG 3350, 20 MM SODIUM CITRATE, PH 5.5. Glutaminyl-5'-O-adenosine phosphoramidate soaking was achieved as follows. 1 uL of a stock solution of 100 mM ligand was added to 2uL of reservoir solution, to achieve a concentration of ~35 mM in the soaking solution. A few RNase A crystals were soaked for 110 - 130 minutes in the soaking solution. Resolution 1.76 Å R-free 0.249

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.

333 other PDB entries and 494 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RNAS1_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–124; UniProt 27–150 Author chain B; PDBConstruct 1–124; UniProt 27–150

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 8uaz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8uaz
Deposition date deposition_date2023-09-22
最后修订 last_revision2024-10-16
Structure title titleStructure of Glutamyl-5'-O-adenosine phosphoramidate/RNase A
Keywords keywords;RNase-A, Nucleotide Prodrug, Amino Acidyl Phosphoramidate, Glutamyl-5'-AMP, Phosphoramidate Hydrolysis, ProTide, HYDROLASE ;; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.39
Radius of gyration Rg (electron density) rg_electron20.97
Forward intensity I(0) i017329900.00
Molecular weight molecular_weight28273.0 kDa
Excluded volume excluded_volume34006 ų
Envelope volume envelope_volume41331 ų
Hydration-shell volume shell_volume17638 ų
Envelope diameter envelope_diameter77.0
Shell Rg shell_rg25.98
Envelope Rg envelope_rg21.20
Shape Rg shape_rg20.95
Total Rg total_rg21.63
Total atoms total_atoms1961
Residues n_residues247
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 dmax76.4
Rg (real space) rg_real21.53
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real1.7330e+07
I(0) uncertainty (real space) i0_real_error2.4200e+05
Rg (reciprocal space) rg_reciprocal21.51
I(0) (reciprocal space) i0_reciprocal17330000.0000
Solution quality estimate total_estimate0.7641
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.5
Skewness Skewness skewness0.503
Kurtosis Kurtosis kurtosis-0.207
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2891000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.728; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.745; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)