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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：Q96AE4 New Search
7PDB entries
12Biological assembly
16chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1J4W COMPLEX OF THE KH3 and KH4 DOMAINS OF FBP WITH A SINGLE_STRANDED 29mer DNA OLIGONUCLEOTIDE FROM THE FUSE ELEMENT OF THE C-MYC ONCOGENE Deposited 2001-11-30 Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: dimeric（2） Consistent with all polymers
Chain A 278–447（170 aa） Fragment：RESIDUES 278-447, NUMBERERED 5-174. KH3 AND KH4 DOMAINS.
Mutation：C59A No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；308 K；Ionic strength (raw mmCIF value) 50 mM SODIUM PHOSPHATE
Resolution not provided
2KXH Solution structure of the first two RRM domains of FIR in the complex with FBP Nbox peptide Deposited 2010-05-05 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 27–52（26 aa） Fragment：UNP residues 27-52
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 8；310 K；Ionic strength (raw mmCIF value) 0.06；Pressure ambient
NMR measurement conditions pH 8；318 K；Ionic strength (raw mmCIF value) 0.06；Pressure ambient
NMR sample composition 0.6 mM [U-15N] protein_1-1, 10 mM TRIS-HCl pH 8.0-2, 50 mM sodium chloride-3, 2 mM TCEP-4, 1.25 mM protein_2-5, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition mM [U-13C; U-15N] protein_1-6, 10 mM TRIS-HCl pH 8.0-7, 50 mM sodium chloride-8, 2 mM TCEP-9, mM protein_2-10, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.3 mM [U-13C; U-15N] protein_2-11, 10 mM TRIS-HCl pH 8.0-12, 50 mM sodium chloride-13, 2 mM TCEP-14, mM protein_1-15, 100% D2O | 100% D2O
NMR sample composition mM [U-13C; U-15N] protein_1-16, 10 mM TRIS-HCl pH 8.0-17, 50 mM sodium chloride-18, 2 mM TCEP-19, mM protein_2-20, 100% D2O | 100% D2O
Resolution not provided
4LIJ Crystal structure of a far upstream element (FUSE) binding protein 1 (FUBP1) from Homo sapiens at 1.95 A resolution Deposited 2013-07-02 Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 86–174（89 aa） Fragment：UNP residues 86-174
Chain B 86–174（89 aa） Fragment：UNP residues 86-174
Chain C 86–174（89 aa） Fragment：UNP residues 86-174
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；277 K；20.00% Glycerol, 1.60M ammonium dihydrogen phosphate, 0.1M TRIS pH 8.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.80 Å R-free 0.199
4LIJ Crystal structure of a far upstream element (FUSE) binding protein 1 (FUBP1) from Homo sapiens at 1.95 A resolution Deposited 2013-07-02 Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain A 86–174（89 aa） Fragment：UNP residues 86-174
Chain B 86–174（89 aa） Fragment：UNP residues 86-174
Chain C 86–174（89 aa） Fragment：UNP residues 86-174
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) PO4 PHOSPHATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；277 K；20.00% Glycerol, 1.60M ammonium dihydrogen phosphate, 0.1M TRIS pH 8.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.80 Å R-free 0.199
6Y24 Crystal structure of fourth KH domain of FUBP1 Deposited 2020-02-14 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 365–455（91 aa）
Not recorded EDO 1,2-ETHANEDIOL × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；3.1 M sodium formate
Resolution 1.86 Å R-free 0.243
6Y2C Crystal structure of the third KH domain of FUBP1 Deposited 2020-02-15 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 260–350（91 aa）
Not recorded EDO 1,2-ETHANEDIOL × 2 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；10% PEG 6000, 10% ethylene glycol, 0.015M Zinkchlorid, 0.1 M MES, pH 6.0
Resolution 2.00 Å R-free 0.240
6Y2C Crystal structure of the third KH domain of FUBP1 Deposited 2020-02-15 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 260–350（91 aa）
Not recorded EDO 1,2-ETHANEDIOL × 6 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；10% PEG 6000, 10% ethylene glycol, 0.015M Zinkchlorid, 0.1 M MES, pH 6.0
Resolution 2.00 Å R-free 0.240
6Y2D Crystal structure of the second KH domain of FUBP1 Deposited 2020-02-15 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 185–259（75 aa）
Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；2M ammonium sulfate, 5% 2-propanol, 2.5% Glycerol
Resolution 1.90 Å R-free 0.239
6Y2D Crystal structure of the second KH domain of FUBP1 Deposited 2020-02-15 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 185–259（75 aa）
Not recorded SO4 SULFATE ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；2M ammonium sulfate, 5% 2-propanol, 2.5% Glycerol
Resolution 1.90 Å R-free 0.239
6Y2D Crystal structure of the second KH domain of FUBP1 Deposited 2020-02-15 Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain C 185–259（75 aa）
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；2M ammonium sulfate, 5% 2-propanol, 2.5% Glycerol
Resolution 1.90 Å R-free 0.239
6Y2D Crystal structure of the second KH domain of FUBP1 Deposited 2020-02-15 Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain D 185–259（75 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；2M ammonium sulfate, 5% 2-propanol, 2.5% Glycerol
Resolution 1.90 Å R-free 0.239
8P25 Solution structure of a chimeric U2AF2 RRM2 / FUBP1 N-Box Deposited 2023-05-14 Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 21–56（36 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 50mM NaCl；Pressure 1
NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] Chimeric construct of U2AF2 linker-RRM2 and FUBP1 N-box, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] Chimeric construct of U2AF2 linker-RRM2 and FUBP1 N-box, 100% D2O | 100% D2O
Resolution not provided

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.