1oia

U1A rnp domain 1-95

Method: X-RAY DIFFRACTION Dmax: 67.3 Å Quality: GOOD

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

U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A

HOMO SAPIENS

UniProt P09012

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 1–95 Fragment:RNP DOMAIN RESIDUES 1-95 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;2M NA/K PHOSPHATE PH 5.5 Resolution 2.40 Å R-free 0.242
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–95 Fragment:RNP DOMAIN RESIDUES 1-95 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;2M NA/K PHOSPHATE PH 5.5 Resolution 2.40 Å R-free 0.242

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.

87 other PDB entries and 144 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RU1A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–95; UniProt 1–95 Author chain B; PDBConstruct 1–95; UniProt 1–95

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 1oia

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1oia
Deposition date deposition_date2003-06-12
Structure title titleU1A rnp domain 1-95
Keywords keywordsRIBONUCLEOPROTEIN, NUCLEAR PROTEIN, RNA-BINDING; RIBONUCLEOPROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.62
Radius of gyration Rg (electron density) rg_electron17.34
Forward intensity I(0) i07299120.00
Molecular weight molecular_weight20402.0 kDa
Excluded volume excluded_volume25906 ų
Envelope volume envelope_volume30953 ų
Hydration-shell volume shell_volume15320 ų
Envelope diameter envelope_diameter70.1
Shell Rg shell_rg23.14
Envelope Rg envelope_rg18.08
Shape Rg shape_rg17.29
Total Rg total_rg18.53
Total atoms total_atoms1437
Residues n_residues176
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 dmax67.3
Rg (real space) rg_real18.64
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real7.2990e+06
I(0) uncertainty (real space) i0_real_error1.0230e+05
Rg (reciprocal space) rg_reciprocal18.64
I(0) (reciprocal space) i0_reciprocal7299000.0000
Solution quality estimate total_estimate0.7593
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.2
Skewness Skewness skewness0.436
Kurtosis Kurtosis kurtosis-0.032
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1870000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.648; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.924; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1oiaa_
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_idd1oiab_
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

CATH v4.4 (2 domains)

Domain ID domain_id1oiaA00
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_id1oiaB00
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)