SAXSdb — 8bwf

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

Polypyrimidine tract-binding protein 1

Homo sapiens

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 57–140	Not recorded	Ligand × 1 SO4 SULFATE ION × 5 NH2 AMINO GROUP × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.86；298 K；1.89M Ammoniumsulfate, 0.1 M HEPES, 2 v/v% PEG400	Resolution 2.90 Å R-free 0.340
10	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain J； UniProt 57–140	Not recorded	Ligand × 1 NH2 AMINO GROUP × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.86；298 K；1.89M Ammoniumsulfate, 0.1 M HEPES, 2 v/v% PEG400	Resolution 2.90 Å R-free 0.340
11	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain K； UniProt 57–140	Not recorded	Ligand × 1 SO4 SULFATE ION × 2 NH2 AMINO GROUP × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.86；298 K；1.89M Ammoniumsulfate, 0.1 M HEPES, 2 v/v% PEG400	Resolution 2.90 Å R-free 0.340
12	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain L； UniProt 57–140	Not recorded	Ligand × 1 SO4 SULFATE ION × 1 NH2 AMINO GROUP × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.86；298 K；1.89M Ammoniumsulfate, 0.1 M HEPES, 2 v/v% PEG400	Resolution 2.90 Å R-free 0.340
13	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain M； UniProt 57–140	Not recorded	Ligand × 1 NH2 AMINO GROUP × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.86；298 K；1.89M Ammoniumsulfate, 0.1 M HEPES, 2 v/v% PEG400	Resolution 2.90 Å R-free 0.340
14	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain N； UniProt 57–140	Not recorded	Ligand × 1 NH2 AMINO GROUP × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.86；298 K；1.89M Ammoniumsulfate, 0.1 M HEPES, 2 v/v% PEG400	Resolution 2.90 Å R-free 0.340
15	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain O； UniProt 57–140	Not recorded	Ligand × 1 SO4 SULFATE ION × 1 NH2 AMINO GROUP × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.86；298 K；1.89M Ammoniumsulfate, 0.1 M HEPES, 2 v/v% PEG400	Resolution 2.90 Å R-free 0.340
16	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain P； UniProt 57–140	Not recorded	Ligand × 1 NH2 AMINO GROUP × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.86；298 K；1.89M Ammoniumsulfate, 0.1 M HEPES, 2 v/v% PEG400	Resolution 2.90 Å R-free 0.340
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 57–140	Not recorded	Ligand × 1 NH2 AMINO GROUP × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.86；298 K；1.89M Ammoniumsulfate, 0.1 M HEPES, 2 v/v% PEG400	Resolution 2.90 Å R-free 0.340
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 57–140	Not recorded	Ligand × 1 SO4 SULFATE ION × 1 NH2 AMINO GROUP × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.86；298 K；1.89M Ammoniumsulfate, 0.1 M HEPES, 2 v/v% PEG400	Resolution 2.90 Å R-free 0.340
4	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 57–140	Not recorded	Ligand × 1 SO4 SULFATE ION × 2 NH2 AMINO GROUP × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.86；298 K；1.89M Ammoniumsulfate, 0.1 M HEPES, 2 v/v% PEG400	Resolution 2.90 Å R-free 0.340
5	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 57–140	Not recorded	Ligand × 1 NH2 AMINO GROUP × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.86；298 K；1.89M Ammoniumsulfate, 0.1 M HEPES, 2 v/v% PEG400	Resolution 2.90 Å R-free 0.340
6	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain F； UniProt 57–140	Not recorded	Ligand × 1 SO4 SULFATE ION × 2 NH2 AMINO GROUP × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.86；298 K；1.89M Ammoniumsulfate, 0.1 M HEPES, 2 v/v% PEG400	Resolution 2.90 Å R-free 0.340
7	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain G； UniProt 57–140	Not recorded	Ligand × 1 SO4 SULFATE ION × 3 NH2 AMINO GROUP × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.86；298 K；1.89M Ammoniumsulfate, 0.1 M HEPES, 2 v/v% PEG400	Resolution 2.90 Å R-free 0.340
8	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain H； UniProt 57–140	Not recorded	Ligand × 1 SO4 SULFATE ION × 1 NH2 AMINO GROUP × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.86；298 K；1.89M Ammoniumsulfate, 0.1 M HEPES, 2 v/v% PEG400	Resolution 2.90 Å R-free 0.340
9	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain I； UniProt 57–140	Not recorded	Ligand × 1 NH2 AMINO GROUP × 1 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.86；298 K；1.89M Ammoniumsulfate, 0.1 M HEPES, 2 v/v% PEG400	Resolution 2.90 Å R-free 0.340

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.

Other PDB	Difference from Current Entry 8BWF	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1QM9 NMR, REPRESENTATIVE STRUCTURE Deposited 1999-09-22	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 335–531（197 aa） Fragment：RNA BINDING FRAGMENT	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5；302 K	Resolution not provided
1SJQ NMR Structure of RRM1 from Human Polypyrimidine Tract Binding Protein Isoform 1 (PTB1) Deposited 2004-03-04	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 54–147（94 aa） Fragment：RRM1, residues 54-147	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；303 K；Ionic strength (raw mmCIF value) 0.3 M；Pressure ambient NMR sample composition 1 mM PTB1-1 U-15N,13C, 50 mM Na phosphate buffer, 100 mM NaCl, 2 mM NaN3,10% D2O \| 100 mM NaCl, 2 mM NaN3,10% D2O	Resolution not provided
1SJR NMR Structure of RRM2 from Human Polypyrimidine Tract Binding Protein Isoform 1 (PTB1) Deposited 2004-03-04	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 147–301（155 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；303 K；Ionic strength (raw mmCIF value) 0.3 M；Pressure ambient NMR sample composition 0.25 mM PTB1-2, U-15N, 13C, 50 mM Na phosphate buffer, 100 mM NaCl, 10 mM DTT, 2 mM NaN3,10% D2O \| 10% D2O	Resolution not provided
2AD9 Solution structure of Polypyrimidine Tract Binding protein RBD1 complexed with CUCUCU RNA Deposited 2005-07-20	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 49–146（98 aa） Fragment：RBD1	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；313 K；Ionic strength (raw mmCIF value) 30mM；Pressure ambient NMR sample composition 1.5mM PTB RBD1 15N, 13C; 1.5mM CUCUCU-RNA; 20mM phosphate buffer; 10mM NaCl \| 90% H2O/10% D2O NMR sample composition 1.5mM PTB RBD1 15N; 1.5mM CUCUCU-RNA; 20mM phosphate buffer; 10mM NaCl \| 90% H2O/10% D2O NMR sample composition 1.5mM PTB RBD1 15N; 1.5mM CUCUCU-RNA; 20mM phosphate buffer; 10mM NaCl \| 100% D2O	Resolution not provided
2ADB Solution structure of Polypyrimidine Tract Binding protein RBD2 complexed with CUCUCU RNA Deposited 2005-07-20	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 172–298（127 aa） Fragment：RBD2	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 5.5；313 K；Ionic strength (raw mmCIF value) 30mM；Pressure ambient NMR sample composition 1.5mM PTB RBD2 15N, 13C; 1.5mM CUCUCU-RNA; 20mM phosphate buffer; 10mM NaCl \| 90% H2O/10% D2O NMR sample composition 1.5mM PTB RBD2 15N; 1.5mM CUCUCU-RNA; 20mM phosphate buffer; 10mM NaCl \| 90% H2O/10% D2O NMR sample composition 1.5mM PTB RBD2 15N; 1.5mM CUCUCU-RNA; 20mM phosphate buffer; 10mM NaCl \| 100% D2O	Resolution not provided
2ADC Solution structure of Polypyrimidine Tract Binding protein RBD34 complexed with CUCUCU RNA Deposited 2005-07-20	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Monomer；Protein × 1 PDB declaration: trimeric	Chain A 324–531（208 aa） Fragment：RBD34	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；313 K；Ionic strength (raw mmCIF value) 30mM；Pressure ambient NMR sample composition 1.5mM PTB RBD34 15N, 13C; 3mM CUCUCU-RNA; 20mM phosphate buffer; 10mM NaCl \| 90% H2O/10% D2O NMR sample composition 1.5mM PTB RBD34 15N; 3mM CUCUCU-RNA; 20mM phosphate buffer; 10mM NaCl \| 90% H2O/10% D2O NMR sample composition 1.5mM PTB RBD34 15N; 3mM CUCUCU-RNA; 20mM phosphate buffer; 10mM NaCl \| 100% D2O	Resolution not provided
2EVZ Structure of RNA Binding Domains 3 and 4 of Polypyrimidine Tract Binding Protein Deposited 2005-11-01	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 324–531（208 aa） Fragment：RNA BINDING DOMAINS 3 AND 4	Not recorded	No recorded non-water small molecule	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
2N3O Structure of PTB RRM1(41-163) bound to an RNA stemloop containing a structured loop derived from viral internal ribosomal entry site RNA Deposited 2015-06-08	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Monomer；Protein × 1 PDB declaration: dimeric	Chain A 41–163（123 aa） Fragment：UNP residues 41-163	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；313 K；Ionic strength (raw mmCIF value) 0.020；Pressure ambient NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 0.020；Pressure ambient NMR measurement conditions pH 6.5；278 K；Ionic strength (raw mmCIF value) 0.020；Pressure ambient NMR measurement conditions pH 6.5；303 K；Ionic strength (raw mmCIF value) 0.020；Pressure ambient NMR sample composition 1 mM [U-99% 15N] PTBRRM1, 1 mM RNA, 10 mM sodium phosphate, 20 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM [U-99% 15N] PTBRRM1, 1 mM [U-99% 13C; U-99% 15N] RNA, 10 mM sodium phosphate, 20 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM [U-99% 15N] PTBRRM1, 1 mM [U-13C; U-15N]-ribose-Cyt9,Ura11,Ura13,Gua15 RNA, 10 mM sodium phosphate, 20 mM sodium chloride, 100% D2O \| 100% D2O NMR sample composition 1 mM [U-99% 15N] PTBRRM1, 1 mM [U-13C; U-15N]-Ura7,Ura10,Cyt11,Ura12,Ura13,Ura14,Cyt15,Cyt16,Ura20,Cyt21,Cyt22,Cyt23 RNA, 10 mM sodium phosphate, 20 mM sodium chloride, 100% D2O \| 100% D2O NMR sample composition 1 mM [U-99% 13C; U-99% 15N] RNA, 10 mM sodium phosphate, 20 mM sodium chloride, 100% D2O \| 100% D2O NMR sample composition 1 mM RNA, 10 mM sodium phosphate, 20 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM [U-99% 13C; U-99% 15N] PTBRRM1, 1 mM RNA, 10 mM sodium phosphate, 20 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM [U-99% 15N] PTBRRM1, 1 mM [U-99% 13C; U-99% 15N] RNA, 10 mM sodium phosphate, 20 mM sodium chloride, 100% D2O \| 100% D2O NMR sample composition 1 mM [U-99% 15N] PTBRRM1, 1 mM [U-13C; U-15N]-ribose-Ura10,Ura12,Ura14 RNA, 10 mM sodium phosphate, 20 mM sodium chloride, 100% D2O \| 100% D2O NMR sample composition 1 mM [U-99% 15N] PTBRRM1, 1 mM RNA, 10 mM sodium phosphate, 20 mM sodium chloride, 100% D2O \| 100% D2O NMR sample composition 1 mM [U-99% 13C; U-99% 15N] PTBRRM1, 1 mM RNA, 10 mM sodium phosphate, 20 mM sodium chloride, 100% D2O \| 100% D2O NMR sample composition 1 mM [U-99% 15N] PTBRRM1, 1 mM RNA, 10 mM sodium phosphate, 20 mM sodium chloride, 13 mg/mL Pf1 phage, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 1 mM [U-99% 15N] PTBRRM1, 1 mM [U-99% 13C; U-99% 15N] RNA, 10 mM sodium phosphate, 20 mM sodium chloride, 13 mg/mL Pf1 phage, 100% D2O \| 100% D2O NMR sample composition 1 mM [U-99% 15N] PTBRRM1, 1 mM [U-99% 13C; U-99% 15N] RNA, 10 mM sodium phosphate, 20 mM sodium chloride, 13 mg/mL Pf1 phage, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
3ZZY Crystal structure of a Raver1 PRI3 peptide in complex with polypyrimidine tract binding protein RRM2 Deposited 2011-09-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 156–285（130 aa） Fragment：RNA RECOGNITION MOTIF 2, RESIDUES 172-301	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；SEE PAPER., pH 6.5	Resolution 1.40 Å R-free 0.234
3ZZY Crystal structure of a Raver1 PRI3 peptide in complex with polypyrimidine tract binding protein RRM2 Deposited 2011-09-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 156–285（130 aa） Fragment：RNA RECOGNITION MOTIF 2, RESIDUES 172-301	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；SEE PAPER., pH 6.5	Resolution 1.40 Å R-free 0.234
3ZZZ Crystal structure of a Raver1 PRI4 peptide in complex with polypyrimidine tract binding protein RRM2 Deposited 2011-09-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 156–285（130 aa） Fragment：RNA RECOGNITION MOTIF 2, RESIDUES 156-285	Not recorded	IOD IODIDE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；SEE PAPER., pH 6.5	Resolution 1.55 Å R-free 0.224
3ZZZ Crystal structure of a Raver1 PRI4 peptide in complex with polypyrimidine tract binding protein RRM2 Deposited 2011-09-06	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 156–285（130 aa） Fragment：RNA RECOGNITION MOTIF 2, RESIDUES 156-285	Not recorded	IOD IODIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；SEE PAPER., pH 6.5	Resolution 1.55 Å R-free 0.224
8BGF NMR solution structure of the N-terminal RRM and flanking linker regions of Polypyrimidine tract binding protein 1 using the CYANA CONSENSUS method. Deposited 2022-10-27	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 41–163（123 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 33.3；Pressure 1 NMR measurement conditions pH 6.5；313 K；Ionic strength (raw mmCIF value) 33.3；Pressure 1 NMR measurement conditions pH 6.5；293 K；Ionic strength (raw mmCIF value) 33.3；Pressure 1 NMR sample composition 0.8 mM [U-15N]-99% Polypyrimidine-tract binding protein N-terminal RNA recognition motif, 10 mM NaH2PO4/NaOH buffer, 20 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.8 mM [U-13C,15N]-99% Polypyrimidine-tract binding protein N-terminal RNA recognition motif, 10 mM NaH2PO4/NaOH buffer, 20 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.8 mM [U-15N]-99% Polypyrimidine-tract binding protein N-terminal RNA recognition motif, 10 mM NaH2PO4/NaOH buffer, 20 mM sodium chloride, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.8 mM [U-15N]-99% Polypyrimidine-tract binding protein N-terminal RNA recognition motif, 10 mM NaH2PO4/NaOH buffer, 20 mM sodium chloride, 0.8 mM [U-13C,15N]-99% UCUUU-SL-RNA, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
9LGQ The crystal structure of SARS-CoV-2 NSP5 in complex with PTBP1 Deposited 2025-01-10	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 316–325（10 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291.15 K；0.1 M MES pH 5.6, 7% PEG 6000, and 6% dimethyl sulfoxide (DMSO)	Resolution 1.82 Å R-free 0.218

12 other PDB entries and 14 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 3–86； UniProt 57–140 Author chain B； PDBConstruct 3–86； UniProt 57–140 Author chain C； PDBConstruct 3–86； UniProt 57–140 Author chain D； PDBConstruct 3–86； UniProt 57–140 Author chain E； PDBConstruct 3–86； UniProt 57–140 Author chain F； PDBConstruct 3–86； UniProt 57–140 Author chain G； PDBConstruct 3–86； UniProt 57–140 Author chain H； PDBConstruct 3–86； UniProt 57–140 Author chain I； PDBConstruct 3–86； UniProt 57–140 Author chain J； PDBConstruct 3–86； UniProt 57–140 Author chain K； PDBConstruct 3–86； UniProt 57–140 Author chain L； PDBConstruct 3–86； UniProt 57–140 Author chain M； PDBConstruct 3–86； UniProt 57–140 Author chain N； PDBConstruct 3–86； UniProt 57–140 Author chain O； PDBConstruct 3–86； UniProt 57–140 Author chain P； PDBConstruct 3–86； UniProt 57–140

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	8bwf
Deposition date deposition_date	2022-12-06
Structure title title	PTBP1 RRM1 bound to an allosteric inhibitor
Keywords keywords	RNA binding, protein-peptide interaction, inhibitor, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	41.68 Å
Radius of gyration Rg (electron density) rg_electron	41.84 Å
Forward intensity I(0) i0	386726000.00
Molecular weight molecular_weight	166580.0 kDa
Excluded volume excluded_volume	211490 Å³
Envelope volume envelope_volume	276030 Å³
Hydration-shell volume shell_volume	56873 Å³
Envelope diameter envelope_diameter	144.8 Å
Shell Rg shell_rg	44.91 Å
Envelope Rg envelope_rg	41.47 Å
Shape Rg shape_rg	41.84 Å
Total Rg total_rg	41.98 Å
Total atoms total_atoms	11678
Residues n_residues	1405
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	143.7 Å
Rg (real space) rg_real	41.95 Å
Rg uncertainty (real space) rg_real_error	1.31 Å
I(0) (real space) i0_real	3.8670e+08
I(0) uncertainty (real space) i0_real_error	7.0200e+06
Rg (reciprocal space) rg_reciprocal	41.68 Å
I(0) (reciprocal space) i0_reciprocal	386600000.0000
Solution quality estimate total_estimate	0.6056
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	41.6 Å
Skewness Skewness skewness	0.539
Kurtosis Kurtosis kurtosis	-0.331
Angular range angular_range	— – 0.1900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	72750000.0000
Real-space data points n_real_points	39
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.692; Stabil: 1.000; Sysdev: 0.046; Positv: 1.000; Valcen: 0.951; Smooth: 0.701

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Polypyrimidine tract-binding protein 1
Molecular weight formula_weight	9612.1 kDa
Source method src_method	man
Copy count entity_count	16

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P
Atom count atom_count	11682

GPPSRVIHIRKLPIDVTEGEVISLGLPFGKVTNLLMLKGKNQAFIEMNTEEAANTMVNYYTSVTPVLRGQPIYIQFSNHKELKTDS

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Ligand
Molecular weight formula_weight	1565.9 kDa
Source method src_method	syn
Copy count entity_count	16

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	a,b,c,d,e,f,g,h,i,j,k,l,m,n,o,p

NQLRAQXALQXVN

Entity 3 Entity 3 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	18

Entity 4 Entity 4 non-polymer

Description description	AMINO GROUP
Molecular weight formula_weight	16.0 kDa
Source method src_method	syn
Copy count entity_count	16

Entity 5 Entity 5 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	nat
Copy count entity_count	4

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8. Citations (1)

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Unit-cell length a length_a	244.200 Å
Unit-cell length b length_b	76.630 Å
Unit-cell length c length_c	94.130 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	64

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	—

Resolution resolution	2.900 Å
Low-resolution limit resolution_low	46.210 Å
R factor r_factor	0.2478
R_work r_work	0.2432
R_free r_free	0.3403

fit	/app/data/saxs_computation/bw/8bwf/8bwf.fit
pddf	/app/data/pr_computation/bw/8bwf/8bwf.pr.out
profile	/app/data/saxs_computation/bw/8bwf/8bwf.dat

PTBP1 RRM1 bound to an allosteric inhibitor

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

Polypyrimidine tract-binding protein 1

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)