2evz

Structure of RNA Binding Domains 3 and 4 of Polypyrimidine Tract Binding Protein

Method: SOLUTION NMR Dmax: 55.0 Å Quality: REASONABLE

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

Polypyrimidine tract-binding protein 1

Homo sapiens

UniProt P26599

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 324–531 Fragment:RNA BINDING DOMAINS 3 AND 4 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.5;303 K;Ionic strength (raw mmCIF value) 20mM NaCl, 10mM Na-phosphate;Pressure 1 NMR sample composition:1mM PTB RBD34 15N; 20mM NaCl; 10mM sodium phosphate; 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:1mM PTB RBD34 15N, 13C; 20mM NaCl; 10mM sodium phosphate; 90% H2O, 10% D2O | 90% H2O/10% D2O NMR sample composition:1mM PTB RBD34 15N; 20mM NaCl; 10mM sodium phosphate; 100% D2O | 100% D2O NMR sample composition:1mM PTB RBD34 15N, 13C; 20mM NaCl; 10mM sodium phosphate; 100% D2O | 100% D2O NMR sample composition:1mM PTB RBD3 15N, 13C, RBD4 unlabeled; 20mM NaCl; 10mM sodium phosphate; 100% D2O | 100% D2O NMR sample composition:1mM PTB RBD3 unlabeled, RBD4 13C, 15N; 20mM NaCl; 10mM sodium phosphate; 100% D2O | 100% D2O Resolution not provided

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.

12 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PTBP1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 22–229; UniProt 324–531

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 2evz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2evz
Deposition date deposition_date2005-11-01
Structure title titleStructure of RNA Binding Domains 3 and 4 of Polypyrimidine Tract Binding Protein
Keywords keywordsALPHA-BETA SANDWICH, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.19
Radius of gyration Rg (electron density) rg_electron17.89
Forward intensity I(0) i02880540000.00
Molecular weight molecular_weight458750.0 kDa
Excluded volume excluded_volume576080 ų
Envelope volume envelope_volume68620 ų
Hydration-shell volume shell_volume25160 ų
Envelope diameter envelope_diameter87.2
Shell Rg shell_rg29.83
Envelope Rg envelope_rg24.20
Shape Rg shape_rg17.86
Total Rg total_rg18.20
Total atoms total_atoms65180
Residues n_residues4160
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 dmax55.0
Rg (real space) rg_real18.09
Rg uncertainty (real space) rg_real_error0.09
I(0) (real space) i0_real2.7980e+09
I(0) uncertainty (real space) i0_real_error2.4460e+07
Rg (reciprocal space) rg_reciprocal18.18
I(0) (reciprocal space) i0_reciprocal2881000000.0000
Solution quality estimate total_estimate0.6891
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary21.6
Skewness Skewness skewness0.293
Kurtosis Kurtosis kurtosis-0.311
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha9.3200
Highest regularization parameter α highest_alpha1438000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.951; Stabil: 0.931; Sysdev: 0.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.335

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2evza1
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_idd2evza2
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_id2evzA01
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_id2evzA02
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)