1m5v

Transition State Stabilization by a Catalytic RNA

Method: X-RAY DIFFRACTION Dmax: 214.9 Å Quality: REASONABLE

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–RNA Monomer Protein × 1 RNA 3 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain C; UniProt 1–100 Fragment:U1A RNA BINDING DOMAIN Mutation:Y31H,Q36R RNA INHIBITOR SUBSTRATE × 1 RNA INHIBITOR SUBSTRATE × 1 RNA HAIRPIN RIBOZYME × 1 CA CALCIUM ION × 13 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;300 K;MPD, ammonium chloride, calcium chloride, pH 5.0, VAPOR DIFFUSION, SITTING DROP at 300K Resolution 2.40 Å R-free 0.265
2 Protein–RNA Monomer Protein × 1 RNA 3 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain F; UniProt 1–100 Fragment:U1A RNA BINDING DOMAIN Mutation:Y31H,Q36R RNA INHIBITOR SUBSTRATE × 1 RNA INHIBITOR SUBSTRATE × 1 RNA HAIRPIN RIBOZYME × 1 CA CALCIUM ION × 21 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5;300 K;MPD, ammonium chloride, calcium chloride, pH 5.0, VAPOR DIFFUSION, SITTING DROP at 300K Resolution 2.40 Å R-free 0.265

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 SNRPA_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain C; PDBConstruct 1–100; UniProt 1–100 Author chain F; PDBConstruct 1–100; UniProt 1–100

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 1m5v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1m5v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1m5v
Deposition date deposition_date2002-07-09
Structure title titleTransition State Stabilization by a Catalytic RNA
Keywords keywords;HAIRPIN RIBOZYME, CATALYTIC RNA, U1A RNA BINDING PROTEIN 2'3'cyclic phosphate, cleaved substrate, TRANSLATION-RNA COMPLEX ;; TRANSLATION/RNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier58.42
Radius of gyration Rg (electron density) rg_electron56.91
Forward intensity I(0) i0328664000.00
Molecular weight molecular_weight96286.0 kDa
Excluded volume excluded_volume97833 ų
Envelope volume envelope_volume184680 ų
Hydration-shell volume shell_volume33499 ų
Envelope diameter envelope_diameter210.4
Shell Rg shell_rg42.98
Envelope Rg envelope_rg56.57
Shape Rg shape_rg56.81
Total Rg total_rg56.71
Total atoms total_atoms6395
Residues n_residues412
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 dmax214.9
Rg (real space) rg_real59.70
Rg uncertainty (real space) rg_real_error3.86
I(0) (real space) i0_real3.2870e+08
I(0) uncertainty (real space) i0_real_error7.3040e+06
Rg (reciprocal space) rg_reciprocal57.29
I(0) (reciprocal space) i0_reciprocal327400000.0000
Solution quality estimate total_estimate0.5995
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.8
Skewness Skewness skewness0.526
Kurtosis Kurtosis kurtosis-0.743
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4735000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.089; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.022; Smooth: 0.502

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1m5vc_
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_idd1m5vf_
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_id1m5vC00
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_id1m5vF00
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)