1syx

The crystal structure of a binary U5 snRNP complex

Method: X-RAY DIFFRACTION Dmax: 141.8 Å Quality: REASONABLE

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

Spliceosomal U5 snRNP-specific 15 kDa protein

Homo sapiens

UniProt P83876

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 1–142 Not recorded CD2 antigen cytoplasmic tail-binding protein 2 × 1 (O95400) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;PEG 2000mme, MES, calcium acetate, 1,4-butanediol, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.35 Å R-free 0.262
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–142 Not recorded CD2 antigen cytoplasmic tail-binding protein 2 × 1 (O95400) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;PEG 2000mme, MES, calcium acetate, 1,4-butanediol, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.35 Å R-free 0.262
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–142 Not recorded CD2 antigen cytoplasmic tail-binding protein 2 × 1 (O95400) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;PEG 2000mme, MES, calcium acetate, 1,4-butanediol, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.35 Å R-free 0.262

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.

31 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TXN4A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–142; UniProt 1–142 Author chain C; PDBConstruct 1–142; UniProt 1–142 Author chain E; PDBConstruct 1–142; UniProt 1–142

CD2 antigen cytoplasmic tail-binding protein 2

Homo sapiens

UniProt O95400

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 B; UniProt 262–341 Fragment:86 amino acid C-terminal fragment Spliceosomal U5 snRNP-specific 15 kDa protein × 1 (P83876) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;PEG 2000mme, MES, calcium acetate, 1,4-butanediol, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.35 Å R-free 0.262
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 262–341 Fragment:86 amino acid C-terminal fragment Spliceosomal U5 snRNP-specific 15 kDa protein × 1 (P83876) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;PEG 2000mme, MES, calcium acetate, 1,4-butanediol, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.35 Å R-free 0.262
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 262–341 Fragment:86 amino acid C-terminal fragment Spliceosomal U5 snRNP-specific 15 kDa protein × 1 (P83876) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;277 K;PEG 2000mme, MES, calcium acetate, 1,4-butanediol, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.35 Å R-free 0.262

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.

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CD2B2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 7–86; UniProt 262–341 Author chain D; PDBConstruct 7–86; UniProt 262–341 Author chain F; PDBConstruct 7–86; UniProt 262–341

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 1syx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1syx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1syx
Deposition date deposition_date2004-04-02
Structure title titleThe crystal structure of a binary U5 snRNP complex
Keywords keywordsGYF-domain; thioredoxin-like; spliceosomal proteins, TRANSLATION-IMMUNE SYSTEM COMPLEX; TRANSLATION/IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier43.56
Radius of gyration Rg (electron density) rg_electron44.77
Forward intensity I(0) i072771700.00
Molecular weight molecular_weight69430.0 kDa
Excluded volume excluded_volume86867 ų
Envelope volume envelope_volume125760 ų
Hydration-shell volume shell_volume28794 ų
Envelope diameter envelope_diameter153.6
Shell Rg shell_rg38.85
Envelope Rg envelope_rg44.17
Shape Rg shape_rg44.76
Total Rg total_rg44.44
Total atoms total_atoms4890
Residues n_residues591
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 dmax141.8
Rg (real space) rg_real44.43
Rg uncertainty (real space) rg_real_error1.77
I(0) (real space) i0_real7.2770e+07
I(0) uncertainty (real space) i0_real_error1.4660e+06
Rg (reciprocal space) rg_reciprocal43.56
I(0) (reciprocal space) i0_reciprocal72700000.0000
Solution quality estimate total_estimate0.6253
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.6
Skewness Skewness skewness0.582
Kurtosis Kurtosis kurtosis-0.637
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3017000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.336; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.121; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1syxa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.8 — spliceosomal protein U5-15Kd
Domain ID domain_idd1syxb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.76 — GYF/BRK domain-like
Superfamily Superfamily superfamilyd.76.1 — GYF domain
Family Family familyd.76.1.1 — GYF domain
Domain ID domain_idd1syxc_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.8 — spliceosomal protein U5-15Kd
Domain ID domain_idd1syxd_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.76 — GYF/BRK domain-like
Superfamily Superfamily superfamilyd.76.1 — GYF domain
Family Family familyd.76.1.1 — GYF domain
Domain ID domain_idd1syxe_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.8 — spliceosomal protein U5-15Kd
Domain ID domain_idd1syxf_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.76 — GYF/BRK domain-like
Superfamily Superfamily superfamilyd.76.1 — GYF domain
Family Family familyd.76.1.1 — GYF domain

CATH v4.4 (6 domains)

Domain ID domain_id1syxA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id1syxB00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1490 — Dna Ligase; domain 1
Homologous superfamily homologous superfamily40 — GYF domain
Domain ID domain_id1syxC00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id1syxD00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1490 — Dna Ligase; domain 1
Homologous superfamily homologous superfamily40 — GYF domain
Domain ID domain_id1syxE00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id1syxF00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1490 — Dna Ligase; domain 1
Homologous superfamily homologous superfamily40 — GYF domain

8. Citations (1)

9. Files and Curves (10)