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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：Q03405 New Search
12PDB entries
17Biological assembly
19chain/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
2FD6 Structure of Human Urokinase Plasminogen Activator in Complex with Urokinase Receptor and an anti-upar antibody at 1.9 A Deposited 2005-12-13 Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain U 23–297（275 aa） Fragment：residues 23-297
Not recorded SO4 SULFATE ION × 1 ETX 2-ETHOXYETHANOL × 3 EDO 1,2-ETHANEDIOL × 2 PGE TRIETHYLENE GLYCOL × 1 NDG 2-acetamido-2-deoxy-alpha-D-glucopyranose × 1 PG4 TETRAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICRODIALYSIS；pH 6.5；298 K；4% PEG4000, 5% ethylene glycol, 5% methanol, 0.05% sodium azide, 50 mM cacodylate, pH 6.5, MICRODIALYSIS, temperature 298K
Resolution 1.90 Å R-free 0.276
2FD6 Structure of Human Urokinase Plasminogen Activator in Complex with Urokinase Receptor and an anti-upar antibody at 1.9 A Deposited 2005-12-13 Assembly 2 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain U 23–297（275 aa） Fragment：residues 23-297
Not recorded SO4 SULFATE ION × 1 ETX 2-ETHOXYETHANOL × 3 EDO 1,2-ETHANEDIOL × 2 PGE TRIETHYLENE GLYCOL × 1 NDG 2-acetamido-2-deoxy-alpha-D-glucopyranose × 1 PG4 TETRAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICRODIALYSIS；pH 6.5；298 K；4% PEG4000, 5% ethylene glycol, 5% methanol, 0.05% sodium azide, 50 mM cacodylate, pH 6.5, MICRODIALYSIS, temperature 298K
Resolution 1.90 Å R-free 0.276
2I9B Crystal structure of ATF-urokinase receptor complex Deposited 2006-09-05 Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain E 23–299（277 aa） Fragment：UPAR, residues 23-299
Mutation：N162Q, N172Q, N200Q, N233Q SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；293 K；22.5% w/v PEG3350, 200 mM ammonium sulfate, 100 mM Bis-Tris, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.80 Å R-free 0.265
2I9B Crystal structure of ATF-urokinase receptor complex Deposited 2006-09-05 Assembly 2 Other combination Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain F 23–299（277 aa） Fragment：UPAR, residues 23-299
Mutation：N162Q, N172Q, N200Q, N233Q SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；293 K；22.5% w/v PEG3350, 200 mM ammonium sulfate, 100 mM Bis-Tris, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.80 Å R-free 0.265
2I9B Crystal structure of ATF-urokinase receptor complex Deposited 2006-09-05 Assembly 3 Other combination Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain G 23–299（277 aa） Fragment：UPAR, residues 23-299
Mutation：N162Q, N172Q, N200Q, N233Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；293 K；22.5% w/v PEG3350, 200 mM ammonium sulfate, 100 mM Bis-Tris, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.80 Å R-free 0.265
2I9B Crystal structure of ATF-urokinase receptor complex Deposited 2006-09-05 Assembly 4 Other combination Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain H 23–299（277 aa） Fragment：UPAR, residues 23-299
Mutation：N162Q, N172Q, N200Q, N233Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；293 K；22.5% w/v PEG3350, 200 mM ammonium sulfate, 100 mM Bis-Tris, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.80 Å R-free 0.265
3BT1 Structure of urokinase receptor, urokinase and vitronectin complex Deposited 2007-12-27 Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain U 23–303（281 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION
X-ray crystallization conditions MICRODIALYSIS；pH 7.5；295 K；12% PEG 3350, 50mM HEPES pH 7.5, MICRODIALYSIS, temperature 295K
Resolution 2.80 Å R-free 0.308
3BT2 Structure of urokinase receptor, urokinase and vitronectin complex Deposited 2007-12-27 Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain U 23–303（281 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICRODIALYSIS；pH 7.5；295 K；8% PEG 4000, 2.5% ethanol, 0.05% sodium azide, 50mM cacodylate pH 6.5, pH 7.5, MICRODIALYSIS, temperature 295K
Resolution 2.50 Å R-free 0.272
3BT2 Structure of urokinase receptor, urokinase and vitronectin complex Deposited 2007-12-27 Assembly 2 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain U 23–303（281 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICRODIALYSIS；pH 7.5；295 K；8% PEG 4000, 2.5% ethanol, 0.05% sodium azide, 50mM cacodylate pH 6.5, pH 7.5, MICRODIALYSIS, temperature 295K
Resolution 2.50 Å R-free 0.272
3U73 Crystal structure of stabilized human uPAR mutant in complex with ATF Deposited 2011-10-13 Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain U 23–305（283 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.4；295 K；0.2M NaCl, 100mM HEPES, pH7.4, 1.8 M ammonium sulfate, vapor diffusion, sitting drop, temperature 295.0K
Resolution 3.19 Å R-free 0.258
3U74 Crystal structure of stabilized human uPAR mutant Deposited 2011-10-13 Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain U 23–305（283 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.4；295 K；100 mM HEPES, pH 7.5, 2% (w/v) PEG400, 2 M ammonium sulfate, vapor diffusion, sitting drop, temperature 295.0K
Resolution 2.39 Å R-free 0.252
4K24 Structure of anti-uPAR Fab ATN-658 in complex with uPAR Deposited 2013-04-08 Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain U 23–303（281 aa） Fragment：UNP residues 23-303
Not recorded MAN alpha-D-mannopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；295 K；0.1M HEPES pH 7.5, 55%(v/v) Tacsimate, 2%(v/v) 2-methyl-1,3-propanediol, vapor diffusion, sitting drop, temperature 295K
Resolution 4.50 Å R-free 0.275
4QTI Crystal structure of human uPAR in complex with anti-uPAR Fab 8B12 Deposited 2014-07-08 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain U 23–305（283 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；298 K；48% MPD, 100mM Tris, 100mM NaCl, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 3.00 Å R-free 0.296
7E17 Structure of dimeric uPAR Deposited 2021-02-01 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 23–299（277 aa）
Chain B 23–299（277 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；295 K；1.8-2.2 M ammonium sulphate in 50 mM sodium acetate at pH 4.5oC5.2
Resolution 2.96 Å R-free 0.299
7V63 Structure of dimeric uPAR at low pH Deposited 2021-08-19 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 23–299（277 aa）
Chain B 23–299（277 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；295 K；1.8-2.2 M ammonium sulphate in 50 mM sodium acetate at pH 4.5-5.2
Resolution 2.91 Å R-free 0.273
9YC5 Human uPAR bound to the Fab fragment of targeted cancer therapeutic antibody FL1 Deposited 2025-09-18 Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 23–305（283 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；20mM Tris, 150mM NaCl, 2.5% Glycerol, 1mM EDTA, pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.94 Å
9YC6 Mutant human uPAR bound to the Fab fragment of the targeted cancer therapeutic antibody FL1 Deposited 2025-09-18 Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain U 23–305（283 aa）
Mutation：H47C, N259C NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；20mM Tris, 150mM NaCl, 2.5% Glycerol, 1mM EDTA, pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.80 Å

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.