3dxb

Structure of the UHM domain of Puf60 fused to thioredoxin

Method: X-RAY DIFFRACTION Dmax: 115.1 Å Quality: EXCELLENT

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

thioredoxin N-terminally fused to Puf60(UHM)

Homo sapiens

UniProt P0AA27

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–109 Chain F; UniProt 1–109 Fragment:Chimera of Thioredoxin 1-109 and Puf60 C-terminal 460-559 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;1.4M ammonium sulfate, 0.05M K-formate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.20 Å R-free 0.271
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–109 Chain D; UniProt 1–109 Fragment:Chimera of Thioredoxin 1-109 and Puf60 C-terminal 460-559 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;1.4M ammonium sulfate, 0.05M K-formate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.20 Å R-free 0.271
3 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–109 Chain G; UniProt 1–109 Fragment:Chimera of Thioredoxin 1-109 and Puf60 C-terminal 460-559 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;1.4M ammonium sulfate, 0.05M K-formate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.20 Å R-free 0.271
4 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–109 Chain H; UniProt 1–109 Fragment:Chimera of Thioredoxin 1-109 and Puf60 C-terminal 460-559 CL CHLORIDE ION × 2 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;1.4M ammonium sulfate, 0.05M K-formate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.20 Å R-free 0.271
5 Insufficient information Homooligomer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–109 Chain B; UniProt 1–109 Chain C; UniProt 1–109 Chain D; UniProt 1–109 Chain E; UniProt 1–109 Chain F; UniProt 1–109 Chain G; UniProt 1–109 Chain H; UniProt 1–109 Fragment:Chimera of Thioredoxin 1-109 and Puf60 C-terminal 460-559 CL CHLORIDE ION × 4 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;1.4M ammonium sulfate, 0.05M K-formate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.20 Å R-free 0.271

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.

4 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name THIO_ECO57
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 10–118; UniProt 1–109 Author chain B; PDBConstruct 10–118; UniProt 1–109 Author chain C; PDBConstruct 10–118; UniProt 1–109 Author chain D; PDBConstruct 10–118; UniProt 1–109 Author chain E; PDBConstruct 10–118; UniProt 1–109 Author chain F; PDBConstruct 10–118; UniProt 1–109 Author chain G; PDBConstruct 10–118; UniProt 1–109 Author chain H; PDBConstruct 10–118; UniProt 1–109

thioredoxin N-terminally fused to Puf60(UHM)

Homo sapiens

UniProt Q9UHX1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 460–499 Chain F; UniProt 460–499 Fragment:Chimera of Thioredoxin 1-109 and Puf60 C-terminal 460-559 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;1.4M ammonium sulfate, 0.05M K-formate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.20 Å R-free 0.271
2 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 460–499 Chain D; UniProt 460–499 Fragment:Chimera of Thioredoxin 1-109 and Puf60 C-terminal 460-559 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;1.4M ammonium sulfate, 0.05M K-formate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.20 Å R-free 0.271
3 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 460–499 Chain G; UniProt 460–499 Fragment:Chimera of Thioredoxin 1-109 and Puf60 C-terminal 460-559 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;1.4M ammonium sulfate, 0.05M K-formate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.20 Å R-free 0.271
4 Insufficient information Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 460–499 Chain H; UniProt 460–499 Fragment:Chimera of Thioredoxin 1-109 and Puf60 C-terminal 460-559 CL CHLORIDE ION × 2 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;1.4M ammonium sulfate, 0.05M K-formate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.20 Å R-free 0.271
5 Insufficient information Homooligomer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 460–499 Chain B; UniProt 460–499 Chain C; UniProt 460–499 Chain D; UniProt 460–499 Chain E; UniProt 460–499 Chain F; UniProt 460–499 Chain G; UniProt 460–499 Chain H; UniProt 460–499 Fragment:Chimera of Thioredoxin 1-109 and Puf60 C-terminal 460-559 CL CHLORIDE ION × 4 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;1.4M ammonium sulfate, 0.05M K-formate, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.20 Å R-free 0.271

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.

13 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PUF60_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 123–162; UniProt 460–499 Author chain B; PDBConstruct 123–162; UniProt 460–499 Author chain C; PDBConstruct 123–162; UniProt 460–499 Author chain D; PDBConstruct 123–162; UniProt 460–499 Author chain E; PDBConstruct 123–162; UniProt 460–499 Author chain F; PDBConstruct 123–162; UniProt 460–499 Author chain G; PDBConstruct 123–162; UniProt 460–499 Author chain H; PDBConstruct 123–162; UniProt 460–499

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 3dxb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3dxb
Deposition date deposition_date2008-07-24
Structure title titleStructure of the UHM domain of Puf60 fused to thioredoxin
Keywords keywordssplicing, FBP interacting repressor, UHM, RRM, Electron transport, Redox-active center, Transport, TRANSCRIPTION; SPLICING, TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.37
Radius of gyration Rg (electron density) rg_electron37.26
Forward intensity I(0) i0520090000.00
Molecular weight molecular_weight186050.0 kDa
Excluded volume excluded_volume233080 ų
Envelope volume envelope_volume322330 ų
Hydration-shell volume shell_volume69465 ų
Envelope diameter envelope_diameter113.8
Shell Rg shell_rg45.98
Envelope Rg envelope_rg35.83
Shape Rg shape_rg37.29
Total Rg total_rg37.72
Total atoms total_atoms13082
Residues n_residues1695
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 dmax115.1
Rg (real space) rg_real38.04
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real5.2010e+08
I(0) uncertainty (real space) i0_real_error8.2140e+06
Rg (reciprocal space) rg_reciprocal38.25
I(0) (reciprocal space) i0_reciprocal520200000.0000
Solution quality estimate total_estimate0.9024
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.5
Skewness Skewness skewness0.014
Kurtosis Kurtosis kurtosis-0.601
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha103500000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.941; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.967; Smooth: 0.936

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

Domain ID domain_id3dxbA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id3dxbA02
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_id3dxbB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id3dxbB02
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_id3dxbC01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id3dxbC02
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_id3dxbD01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id3dxbD02
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_id3dxbE01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id3dxbE02
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_id3dxbF01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id3dxbF02
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_id3dxbG01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id3dxbG02
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_id3dxbH01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id3dxbH02
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 (2)

9. Files and Curves (10)