2w5i

RNASE A-AP3A COMPLEX

Method: X-RAY DIFFRACTION Dmax: 77.4 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 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;20% PEG 4000, 0.02M SODIUM CITRATE BUFFER, PH 5.5 Resolution 2.40 Å R-free 0.273
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 27–150 Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;20% PEG 4000, 0.02M SODIUM CITRATE BUFFER, PH 5.5 Resolution 2.40 Å R-free 0.273

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 2w5i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2w5i
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2w5i
Deposition date deposition_date2008-12-10
Structure title titleRNASE A-AP3A COMPLEX
Keywords keywordsGLYCOPROTEIN, ENDONUCLEASE, HYDROLASE, INHIBITOR, NUCLEOTIDE ATP, ENZYME, NUCLEASE, SECRETED, GLYCATION; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.26
Radius of gyration Rg (electron density) rg_electron20.80
Forward intensity I(0) i016732200.00
Molecular weight molecular_weight27223.0 kDa
Excluded volume excluded_volume32443 ų
Envelope volume envelope_volume40032 ų
Hydration-shell volume shell_volume17268 ų
Envelope diameter envelope_diameter76.1
Shell Rg shell_rg25.71
Envelope Rg envelope_rg20.99
Shape Rg shape_rg20.81
Total Rg total_rg21.40
Total atoms total_atoms1885
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 dmax77.4
Rg (real space) rg_real21.41
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.6730e+07
I(0) uncertainty (real space) i0_real_error2.4600e+05
Rg (reciprocal space) rg_reciprocal21.38
I(0) (reciprocal space) i0_reciprocal16730000.0000
Solution quality estimate total_estimate0.8283
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.6
Skewness Skewness skewness0.512
Kurtosis Kurtosis kurtosis-0.174
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2869000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.698; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.689; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2w5ia_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.5 — RNase A-like
Superfamily Superfamily superfamilyd.5.1 — RNase A-like
Family Family familyd.5.1.1 — Ribonuclease A-like
Domain ID domain_idd2w5ib_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.5 — RNase A-like
Superfamily Superfamily superfamilyd.5.1 — RNase A-like
Family Family familyd.5.1.1 — Ribonuclease A-like

CATH v4.4 (2 domains)

Domain ID domain_id2w5iA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology130 — P-30 Protein
Homologous superfamily homologous superfamily10 — Ribonuclease A-like domain
Domain ID domain_id2w5iB00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology130 — P-30 Protein
Homologous superfamily homologous superfamily10 — Ribonuclease A-like domain

8. Citations (1)

9. Files and Curves (10)