2f9d

2.5 angstrom resolution structure of the spliceosomal protein p14 bound to region of SF3b155

Method: X-RAY DIFFRACTION Dmax: 81.3 Å Quality: GOOD

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

Pre-mRNA branch site protein p14

Homo sapiens

UniProt Q9Y3B4

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–125 Not recorded Splicing factor 3B subunit 1 × 1 (O75533) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;14-18% PEG3350, MOPS buffer, 0.2M sodium formate selenomethionine derivatized SF3b155 protein, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.50 Å R-free 0.276
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–125 Not recorded Splicing factor 3B subunit 1 × 1 (O75533) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;14-18% PEG3350, MOPS buffer, 0.2M sodium formate selenomethionine derivatized SF3b155 protein, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.50 Å R-free 0.276

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.

38 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PM14_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–125; UniProt 1–125 Author chain B; PDBConstruct 1–125; UniProt 1–125

Splicing factor 3B subunit 1

Homo sapiens

UniProt O75533

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain P; UniProt 373–415 Fragment:Residues: 373-415 Non-standard monomer:Yes (specific site not provided by mmCIF) Pre-mRNA branch site protein p14 × 1 (Q9Y3B4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;14-18% PEG3350, MOPS buffer, 0.2M sodium formate selenomethionine derivatized SF3b155 protein, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.50 Å R-free 0.276
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain Q; UniProt 373–415 Fragment:Residues: 373-415 Non-standard monomer:Yes (specific site not provided by mmCIF) Pre-mRNA branch site protein p14 × 1 (Q9Y3B4) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;14-18% PEG3350, MOPS buffer, 0.2M sodium formate selenomethionine derivatized SF3b155 protein, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.50 Å R-free 0.276

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.

71 other PDB entries and 76 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SF3B1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 1–43; UniProt 373–415 Author chain Q; PDBConstruct 1–43; UniProt 373–415

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 2f9d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2f9d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2f9d
Deposition date deposition_date2005-12-05
Structure title title2.5 angstrom resolution structure of the spliceosomal protein p14 bound to region of SF3b155
Keywords keywordsp14 SF3bp14 SF3b155 SAP155 RRM, 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_guinier23.39
Radius of gyration Rg (electron density) rg_electron22.46
Forward intensity I(0) i023225000.00
Molecular weight molecular_weight36521.0 kDa
Excluded volume excluded_volume45631 ų
Envelope volume envelope_volume57243 ų
Hydration-shell volume shell_volume21963 ų
Envelope diameter envelope_diameter83.8
Shell Rg shell_rg28.29
Envelope Rg envelope_rg22.82
Shape Rg shape_rg22.39
Total Rg total_rg23.43
Total atoms total_atoms2560
Residues n_residues302
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 dmax81.3
Rg (real space) rg_real23.41
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real2.3220e+07
I(0) uncertainty (real space) i0_real_error3.0070e+05
Rg (reciprocal space) rg_reciprocal23.40
I(0) (reciprocal space) i0_reciprocal23220000.0000
Solution quality estimate total_estimate0.8722
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.3
Skewness Skewness skewness0.367
Kurtosis Kurtosis kurtosis-0.272
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4220000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.796; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.952; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd2f9da1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.7 — RNA-binding domain, RBD, aka RNA recognition motif (RRM)
Family Family familyd.58.7.1 — Canonical RBD
Domain ID domain_idd2f9db_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.7 — RNA-binding domain, RBD, aka RNA recognition motif (RRM)
Family Family familyd.58.7.1 — Canonical RBD
Domain ID domain_idd2f9dp_
Class classj — Peptides
Fold Fold foldj.148 — Splicing factor 3B subunit 1 fragment
Superfamily Superfamily superfamilyj.148.1 — Splicing factor 3B subunit 1 fragment
Family Family familyj.148.1.1 — Splicing factor 3B subunit 1 fragment
Domain ID domain_idd2f9dq_
Class classj — Peptides
Fold Fold foldj.148 — Splicing factor 3B subunit 1 fragment
Superfamily Superfamily superfamilyj.148.1 — Splicing factor 3B subunit 1 fragment
Family Family familyj.148.1.1 — Splicing factor 3B subunit 1 fragment

CATH v4.4 (2 domains)

Domain ID domain_id2f9dA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain
Domain ID domain_id2f9dB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain

8. Citations (1)

9. Files and Curves (10)