3zzy

Crystal structure of a Raver1 PRI3 peptide in complex with polypyrimidine tract binding protein RRM2

Method: X-RAY DIFFRACTION Dmax: 62.4 Å Quality: GOOD

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 156–285 Fragment:RNA RECOGNITION MOTIF 2, RESIDUES 172-301 RIBONUCLEOPROTEIN PTB-BINDING 1 × 1 (Q9CW46) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;SEE PAPER., pH 6.5 Resolution 1.40 Å R-free 0.234
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 156–285 Fragment:RNA RECOGNITION MOTIF 2, RESIDUES 172-301 RIBONUCLEOPROTEIN PTB-BINDING 1 × 1 (Q9CW46) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;SEE PAPER., pH 6.5 Resolution 1.40 Å R-free 0.234

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 28 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 1–130; UniProt 156–285 Author chain B; PDBConstruct 1–130; UniProt 156–285

RIBONUCLEOPROTEIN PTB-BINDING 1

MUS MUSCULUS

UniProt Q9CW46

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 C; UniProt 496–507 Fragment:MOTIF PRI3, RESIDUES 496-507 Mutation:YES POLYPYRIMIDINE TRACT-BINDING PROTEIN 1 × 1 (P26599) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;SEE PAPER., pH 6.5 Resolution 1.40 Å R-free 0.234
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 496–507 Fragment:MOTIF PRI3, RESIDUES 496-507 Mutation:YES POLYPYRIMIDINE TRACT-BINDING PROTEIN 1 × 1 (P26599) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;SEE PAPER., pH 6.5 Resolution 1.40 Å R-free 0.234

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.

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAVR1_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 5–16; UniProt 496–507 Author chain D; PDBConstruct 5–16; UniProt 496–507

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 3zzy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3zzy
Deposition date deposition_date2011-09-06
Structure title titleCrystal structure of a Raver1 PRI3 peptide in complex with polypyrimidine tract binding protein RRM2
Keywords keywordsPROTEIN BINDING, PEPTIDE BINDING, RNA RECOGNITION MOTIF; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.27
Radius of gyration Rg (electron density) rg_electron18.22
Forward intensity I(0) i010116300.00
Molecular weight molecular_weight24627.0 kDa
Excluded volume excluded_volume31276 ų
Envelope volume envelope_volume36296 ų
Hydration-shell volume shell_volume16886 ų
Envelope diameter envelope_diameter63.2
Shell Rg shell_rg24.05
Envelope Rg envelope_rg18.38
Shape Rg shape_rg18.21
Total Rg total_rg19.23
Total atoms total_atoms1741
Residues n_residues226
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 dmax62.4
Rg (real space) rg_real19.20
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real1.0120e+07
I(0) uncertainty (real space) i0_real_error1.2410e+05
Rg (reciprocal space) rg_reciprocal19.21
I(0) (reciprocal space) i0_reciprocal10120000.0000
Solution quality estimate total_estimate0.8177
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.241
Kurtosis Kurtosis kurtosis-0.383
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1281000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.875; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3zzya_
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_idd3zzyb_
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_id3zzyA00
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_id3zzyB00
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)