3enb

Crystal Structure of PRP8 core domain IV

Method: X-RAY DIFFRACTION Dmax: 79.1 Å Quality: GOOD

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

Pre-mRNA-processing-splicing factor 8

Homo sapiens

UniProt Q6P2Q9

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 1769–1990 Fragment:UNP residues 1769-1990 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;296 K;2.5 M NaCl, 100 mM Tris-HCl pH 7.0, 100 mM MgCl2, VAPOR DIFFUSION, HANGING DROP, temperature 296K Resolution 1.85 Å R-free 0.243
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1769–1990 Fragment:UNP residues 1769-1990 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;296 K;2.5 M NaCl, 100 mM Tris-HCl pH 7.0, 100 mM MgCl2, VAPOR DIFFUSION, HANGING DROP, temperature 296K Resolution 1.85 Å R-free 0.243

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.

100 other PDB entries and 111 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRP8_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–222; UniProt 1769–1990 Author chain B; PDBConstruct 1–222; UniProt 1769–1990

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 3enb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3enb
Deposition date deposition_date2008-09-25
Structure title titleCrystal Structure of PRP8 core domain IV
Keywords keywords;PRP8 domain IV, beta finger, RNase H, spliceosome, U5-220K, Disease mutation, mRNA processing, mRNA splicing, Nucleus, Phosphoprotein, Retinitis pigmentosa, RNA-binding, Sensory transduction, Vision, RNA BINDING PROTEIN ;; RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.51
Radius of gyration Rg (electron density) rg_electron23.34
Forward intensity I(0) i033757100.00
Molecular weight molecular_weight48591.0 kDa
Excluded volume excluded_volume62643 ų
Envelope volume envelope_volume75586 ų
Hydration-shell volume shell_volume26945 ų
Envelope diameter envelope_diameter79.9
Shell Rg shell_rg30.55
Envelope Rg envelope_rg23.70
Shape Rg shape_rg23.31
Total Rg total_rg24.40
Total atoms total_atoms3439
Residues n_residues422
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 dmax79.1
Rg (real space) rg_real24.43
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real3.3760e+07
I(0) uncertainty (real space) i0_real_error3.9960e+05
Rg (reciprocal space) rg_reciprocal24.45
I(0) (reciprocal space) i0_reciprocal33760000.0000
Solution quality estimate total_estimate0.8937
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.1
Skewness Skewness skewness0.293
Kurtosis Kurtosis kurtosis-0.248
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6670000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.878; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.981

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_idd3enba1
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_idd3enbb_
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_id3enbA01
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_id3enbA02
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_id3enbB01
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_id3enbB02
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)