3e9p

Crystal Structure of Yeast Prp8, Residues 1827-2092

Method: X-RAY DIFFRACTION Dmax: 88.2 Å Quality: GOOD

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

Pre-mRNA-splicing factor 8

Saccharomyces cerevisiae

UniProt P33334

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 1833–2087 Fragment:RNA binding domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.10 Å R-free 0.298
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1833–2087 Fragment:RNA binding domain No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.10 Å R-free 0.298

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.

435 other PDB entries and 442 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRP8_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–255; UniProt 1833–2087 Author chain B; PDBConstruct 1–255; UniProt 1833–2087

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 3e9p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3e9p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3e9p
Deposition date deposition_date2008-08-22
Structure title titleCrystal Structure of Yeast Prp8, Residues 1827-2092
Keywords keywords;nucleotidyl transfer, mRNA processing, mRNA splicing, Nucleus, Phosphoprotein, RNA-binding, Spliceosome, RNA BINDING PROTEIN, SPLICING ;; RNA BINDING PROTEIN, SPLICING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.94
Radius of gyration Rg (electron density) rg_electron25.91
Forward intensity I(0) i052008300.00
Molecular weight molecular_weight58470.0 kDa
Excluded volume excluded_volume74348 ų
Envelope volume envelope_volume91212 ų
Hydration-shell volume shell_volume29729 ų
Envelope diameter envelope_diameter91.2
Shell Rg shell_rg32.88
Envelope Rg envelope_rg26.14
Shape Rg shape_rg25.91
Total Rg total_rg26.69
Total atoms total_atoms4120
Residues n_residues510
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 dmax88.2
Rg (real space) rg_real26.95
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real5.2010e+07
I(0) uncertainty (real space) i0_real_error6.8670e+05
Rg (reciprocal space) rg_reciprocal26.95
I(0) (reciprocal space) i0_reciprocal52010000.0000
Solution quality estimate total_estimate0.8898
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.9
Skewness Skewness skewness0.374
Kurtosis Kurtosis kurtosis-0.340
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha10240000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.869; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.975

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3e9pa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.3 — Ribonuclease H-like
Family Family familyc.55.3.14 — Prp8 beta-finger domain-like
Domain ID domain_idd3e9pb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.3 — Ribonuclease H-like
Family Family familyc.55.3.14 — Prp8 beta-finger domain-like

CATH v4.4 (4 domains)

Domain ID domain_id3e9pA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily230 — Prp8 RNase H domain, palm region
Domain ID domain_id3e9pA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology80 — Acyl-CoA Binding Protein
Homologous superfamily homologous superfamily40 — Prp8 RNase H domain, fingers region
Domain ID domain_id3e9pB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily230 — Prp8 RNase H domain, palm region
Domain ID domain_id3e9pB02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology80 — Acyl-CoA Binding Protein
Homologous superfamily homologous superfamily40 — Prp8 RNase H domain, fingers region

8. Citations (1)

9. Files and Curves (10)