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4gp0

The crystal structure of human fascin 1 R149A K150A R151A mutant

Method: X-RAY DIFFRACTION Dmax: 107.4 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Fascin

Homo sapiens

UniProt Q16658

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 1–493 Mutation：R149A K150A R151A BR BROMIDE ION × 1 CL CHLORIDE ION × 11 GOL GLYCEROL × 4 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Hepes, 16% PEG 4000, 1% isopropanol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.50 Å R-free 0.249
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain B； UniProt 1–493 Mutation：R149A K150A R151A BR BROMIDE ION × 6 CL CHLORIDE ION × 18 GOL GLYCEROL × 6 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Hepes, 16% PEG 4000, 1% isopropanol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.50 Å R-free 0.249
3 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 1–493 Chain B； UniProt 1–493 Mutation：R149A K150A R151A BR BROMIDE ION × 14 CL CHLORIDE ION × 58 GOL GLYCEROL × 20 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 6 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Hepes, 16% PEG 4000, 1% isopropanol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.50 Å R-free 0.249

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 4GP0 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1DFC CRYSTAL STRUCTURE OF HUMAN FASCIN, AN ACTIN-CROSSLINKING PROTEIN Deposited 1999-11-18 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–493（493 aa） Fragment：FULL-LENGTH PROTEIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, hepes, dtt, sodium azide , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 2.90 Å R-free 0.268
1DFC CRYSTAL STRUCTURE OF HUMAN FASCIN, AN ACTIN-CROSSLINKING PROTEIN Deposited 1999-11-18 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–493（493 aa） Fragment：FULL-LENGTH PROTEIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, hepes, dtt, sodium azide , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 2.90 Å R-free 0.268
3LLP 1.8 Angstrom human fascin 1 crystal structure Deposited 2010-01-29 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–493（493 aa）
Not recorded GOL GLYCEROL × 3 K POTASSIUM ION × 1 BR BROMIDE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM Hepes, pH 7.5, 20% PEG 4000, 2% isopropanol, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.80 Å R-free 0.220
3LLP 1.8 Angstrom human fascin 1 crystal structure Deposited 2010-01-29 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–493（493 aa）
Not recorded GOL GLYCEROL × 2 K POTASSIUM ION × 1 BR BROMIDE ION × 4 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；100mM Hepes, pH 7.5, 20% PEG 4000, 2% isopropanol, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.80 Å R-free 0.220
3P53 Structure of fascin Deposited 2010-10-07 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–493（493 aa）
Not recorded GOL GLYCEROL × 4 12P DODECAETHYLENE GLYCOL × 1 1PE PENTAETHYLENE GLYCOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；24% PEG 3350, 0.2 M Lithium Acetate, 1mM DTT, 4% glycerol, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.00 Å R-free 0.220
3P53 Structure of fascin Deposited 2010-10-07 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–493（493 aa）
Not recorded GOL GLYCEROL × 4 1PE PENTAETHYLENE GLYCOL × 2 PG0 2-(2-METHOXYETHOXY)ETHANOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；24% PEG 3350, 0.2 M Lithium Acetate, 1mM DTT, 4% glycerol, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.00 Å R-free 0.220
4GOV The crystal structure of human fascin 1 S39D mutant Deposited 2012-08-20 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–493（493 aa）
Mutation：S39D BR BROMIDE ION × 2 CL CHLORIDE ION × 5 GOL GLYCEROL × 3 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100 mM Hepes, 16% PEG 4000, 1% isopropanol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.20 Å R-free 0.234
4GOV The crystal structure of human fascin 1 S39D mutant Deposited 2012-08-20 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–493（493 aa）
Mutation：S39D BR BROMIDE ION × 4 CL CHLORIDE ION × 8 GOL GLYCEROL × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100 mM Hepes, 16% PEG 4000, 1% isopropanol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.20 Å R-free 0.234
4GOV The crystal structure of human fascin 1 S39D mutant Deposited 2012-08-20 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1–493（493 aa）
Chain B 1–493（493 aa）
Mutation：S39D Mutation：S39D BR BROMIDE ION × 12 CL CHLORIDE ION × 26 GOL GLYCEROL × 20 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100 mM Hepes, 16% PEG 4000, 1% isopropanol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.20 Å R-free 0.234
4GOY The crystal structure of human fascin 1 K41A mutant Deposited 2012-08-20 Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–493（493 aa）
Mutation：K41A BR BROMIDE ION × 3 CL CHLORIDE ION × 4 GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Hepes, 16% PEG 4000, 1% isopropanol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.30 Å R-free 0.245
4GOY The crystal structure of human fascin 1 K41A mutant Deposited 2012-08-20 Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–493（493 aa）
Mutation：K41A BR BROMIDE ION × 5 CL CHLORIDE ION × 6 GOL GLYCEROL × 3 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Hepes, 16% PEG 4000, 1% isopropanol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.30 Å R-free 0.245
4GOY The crystal structure of human fascin 1 K41A mutant Deposited 2012-08-20 Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–493（493 aa）
Chain B 1–493（493 aa）
Mutation：K41A Mutation：K41A BR BROMIDE ION × 8 CL CHLORIDE ION × 10 GOL GLYCEROL × 6 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Hepes, 16% PEG 4000, 1% isopropanol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.30 Å R-free 0.245
4GOY The crystal structure of human fascin 1 K41A mutant Deposited 2012-08-20 Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 1–493（493 aa）
Mutation：K41A BR BROMIDE ION × 10 CL CHLORIDE ION × 12 GOL GLYCEROL × 6 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Hepes, 16% PEG 4000, 1% isopropanol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.30 Å R-free 0.245
4GP3 The crystal structure of human fascin 1 K358A mutant Deposited 2012-08-20 Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–493（493 aa）
Mutation：K358A BR BROMIDE ION × 3 CL CHLORIDE ION × 5 GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Hepes, 16% PEG 4000, 1% isopropanol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.25 Å R-free 0.252
4GP3 The crystal structure of human fascin 1 K358A mutant Deposited 2012-08-20 Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–493（493 aa）
Mutation：K358A BR BROMIDE ION × 4 CL CHLORIDE ION × 13 GOL GLYCEROL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Hepes, 16% PEG 4000, 1% isopropanol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.25 Å R-free 0.252
4GP3 The crystal structure of human fascin 1 K358A mutant Deposited 2012-08-20 Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–493（493 aa）
Chain B 1–493（493 aa）
Mutation：K358A Mutation：K358A BR BROMIDE ION × 7 CL CHLORIDE ION × 18 GOL GLYCEROL × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Hepes, 16% PEG 4000, 1% isopropanol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.25 Å R-free 0.252
4GP3 The crystal structure of human fascin 1 K358A mutant Deposited 2012-08-20 Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain B 1–493（493 aa）
Mutation：K358A BR BROMIDE ION × 8 CL CHLORIDE ION × 26 GOL GLYCEROL × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；100mM Hepes, 16% PEG 4000, 1% isopropanol , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.25 Å R-free 0.252
6B0T Structural Insights into the Induced-fit Inhibition of Fascin by a Small Molecule Deposited 2017-09-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 7–493（487 aa） Fragment：residues 7-493
Not recorded C7V 4-methyl-N-(1-{[4-(trifluoromethyl)phenyl]methyl}-1H-indazol-3-yl)-1,2-oxazole-5-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292 K；24% PEG 4000, 50mM Tris HCL (pH 8), 3.3% glycerol, 142mM NaCl, 5mM MgCl2, 10mM CaCl2 and 0.004% NaN3
Resolution 2.80 Å R-free 0.303
6B0T Structural Insights into the Induced-fit Inhibition of Fascin by a Small Molecule Deposited 2017-09-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 7–493（487 aa） Fragment：residues 7-493
Not recorded C7V 4-methyl-N-(1-{[4-(trifluoromethyl)phenyl]methyl}-1H-indazol-3-yl)-1,2-oxazole-5-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292 K；24% PEG 4000, 50mM Tris HCL (pH 8), 3.3% glycerol, 142mM NaCl, 5mM MgCl2, 10mM CaCl2 and 0.004% NaN3
Resolution 2.80 Å R-free 0.303
6B0T Structural Insights into the Induced-fit Inhibition of Fascin by a Small Molecule Deposited 2017-09-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 7–493（487 aa） Fragment：residues 7-493
Not recorded C7V 4-methyl-N-(1-{[4-(trifluoromethyl)phenyl]methyl}-1H-indazol-3-yl)-1,2-oxazole-5-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292 K；24% PEG 4000, 50mM Tris HCL (pH 8), 3.3% glycerol, 142mM NaCl, 5mM MgCl2, 10mM CaCl2 and 0.004% NaN3
Resolution 2.80 Å R-free 0.303
6B0T Structural Insights into the Induced-fit Inhibition of Fascin by a Small Molecule Deposited 2017-09-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 7–493（487 aa） Fragment：residues 7-493
Not recorded C7V 4-methyl-N-(1-{[4-(trifluoromethyl)phenyl]methyl}-1H-indazol-3-yl)-1,2-oxazole-5-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292 K；24% PEG 4000, 50mM Tris HCL (pH 8), 3.3% glycerol, 142mM NaCl, 5mM MgCl2, 10mM CaCl2 and 0.004% NaN3
Resolution 2.80 Å R-free 0.303
6B0T Structural Insights into the Induced-fit Inhibition of Fascin by a Small Molecule Deposited 2017-09-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain E 7–493（487 aa） Fragment：residues 7-493
Not recorded C7V 4-methyl-N-(1-{[4-(trifluoromethyl)phenyl]methyl}-1H-indazol-3-yl)-1,2-oxazole-5-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292 K；24% PEG 4000, 50mM Tris HCL (pH 8), 3.3% glycerol, 142mM NaCl, 5mM MgCl2, 10mM CaCl2 and 0.004% NaN3
Resolution 2.80 Å R-free 0.303
6B0T Structural Insights into the Induced-fit Inhibition of Fascin by a Small Molecule Deposited 2017-09-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain F 7–493（487 aa） Fragment：residues 7-493
Not recorded C7V 4-methyl-N-(1-{[4-(trifluoromethyl)phenyl]methyl}-1H-indazol-3-yl)-1,2-oxazole-5-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；292 K；24% PEG 4000, 50mM Tris HCL (pH 8), 3.3% glycerol, 142mM NaCl, 5mM MgCl2, 10mM CaCl2 and 0.004% NaN3
Resolution 2.80 Å R-free 0.303
6I0Z CRYSTAL STRUCTURE OF FASCIN IN COMPLEX WITH COMPOUND 1 Deposited 2018-10-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–493（493 aa）
Not recorded GZQ ~{N}-(2,4-dichlorophenyl)-~{N}-methyl-ethanamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；292 K；16-20% PEG 3350, 200 mM LiAc, 4% glycerol
Resolution 1.77 Å R-free 0.227
6I0Z CRYSTAL STRUCTURE OF FASCIN IN COMPLEX WITH COMPOUND 1 Deposited 2018-10-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–493（493 aa）
Not recorded GZQ ~{N}-(2,4-dichlorophenyl)-~{N}-methyl-ethanamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；292 K；16-20% PEG 3350, 200 mM LiAc, 4% glycerol
Resolution 1.77 Å R-free 0.227
6I10 CRYSTAL STRUCTURE OF FASCIN IN COMPLEX WITH COMPOUND 2 Deposited 2018-10-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–493（493 aa）
Not recorded GZK 1-[(3~{R})-1,1-bis(oxidanylidene)thiolan-3-yl]-5-[(3,4-dichlorophenyl)methyl]pyrazolo[3,4-d]pyrimidin-4-one × 1 ACT ACETATE ION × 1 EDO 1,2-ETHANEDIOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；292 K；18-22% PEG 8000, 100-130 mM MgAc2, 100 mM citric acid pH 5.0
Resolution 2.10 Å R-free 0.287
6I11 CRYSTAL STRUCTURE OF FASCIN IN COMPLEX WITH COMPOUND 3 Deposited 2018-10-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–493（493 aa）
Not recorded ACT ACETATE ION × 1 H0H ~{N}-(1-methylpyrazol-4-yl)-1-oxidanylidene-2-(phenylmethyl)isoquinoline-4-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；292 K；18-22% PEG 8000, 100-130 mM MgAc2, 100 mM citric acid pH 5.0
Resolution 1.67 Å R-free 0.247
6I12 CRYSTAL STRUCTURE OF FASCIN IN COMPLEX WITH COMPOUND 5 Deposited 2018-10-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–493（493 aa）
Not recorded ACT ACETATE ION × 1 H08 2-[(4-chlorophenyl)methyl]-~{N}-(1-methylpyrazol-4-yl)-1-oxidanylidene-isoquinoline-4-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；292 K；18-22% PEG 8000, 100-130 mM MgAc2, 100 mM citric acid pH 5.0
Resolution 1.65 Å R-free 0.208
6I13 CRYSTAL STRUCTURE OF FASCIN IN COMPLEX WITH COMPOUND 7 Deposited 2018-10-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–493（493 aa）
Not recorded ACT ACETATE ION × 1 EDO 1,2-ETHANEDIOL × 3 H0Q 2-[(3-chlorophenyl)methyl]-~{N}-(1-methylpyrazol-4-yl)-1-oxidanylidene-isoquinoline-4-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；292 K；18-22% PEG 8000, 100-130 mM MgAc2, 100 mM citric acid pH 5.0
Resolution 1.79 Å R-free 0.227
6I14 CRYSTAL STRUCTURE OF FASCIN IN COMPLEX WITH COMPOUND 9 Deposited 2018-10-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–493（493 aa）
Not recorded ACT ACETATE ION × 1 GZN 2-[(3,4-dichlorophenyl)methyl]-~{N}-(1-methylpyrazol-4-yl)-1-oxidanylidene-isoquinoline-4-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；292 K；18-22% PEG 8000, 100-130 mM MgAc2, 100 mM citric acid pH 5.0
Resolution 1.73 Å R-free 0.216
6I15 CRYSTAL STRUCTURE OF FASCIN IN COMPLEX WITH COMPOUND 11 Deposited 2018-10-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–493（493 aa）
Not recorded EDO 1,2-ETHANEDIOL × 2 ACT ACETATE ION × 1 GZT 1-[[2,2-bis(fluoranyl)-1,3-benzodioxol-5-yl]methyl]-~{N}-methyl-2-oxidanylidene-pyridine-3-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；292 K；18-22% PEG 8000, 100-130 mM MgAc2, 100 mM citric acid pH 5.0
Resolution 1.91 Å R-free 0.243
6I16 CRYSTAL STRUCTURE OF FASCIN IN COMPLEX WITH COMPOUND 15 Deposited 2018-10-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–493（493 aa）
Not recorded ACT ACETATE ION × 1 H0B 6-[(3,4-dichlorophenyl)methyl]-~{N}-(1-methylpyrazol-4-yl)-5-oxidanylidene-1,6-naphthyridine-8-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；292 K；18-22% PEG 8000, 100-130 mM MgAc2, 100 mM citric acid pH 5.0
Resolution 2.00 Å R-free 0.239
6I17 CRYSTAL STRUCTURE OF FASCIN IN COMPLEX WITH COMPOUND 24 Deposited 2018-10-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–493（493 aa）
Not recorded ACT ACETATE ION × 1 EDO 1,2-ETHANEDIOL × 1 GZW 2-[(3,4-dichlorophenyl)methyl]-~{N}-(1-methylpyrazol-4-yl)-1-oxidanylidene-6-piperidin-4-yl-2,7-naphthyridine-4-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；292 K；18-22% PEG 8000, 100-130 mM MgAc2, 100 mM citric acid pH 5.0
Resolution 1.56 Å R-free 0.240
6I18 CRYSTAL STRUCTURE OF FASCIN IN COMPLEX WITH BDP-13176 Deposited 2018-10-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–493（493 aa）
Not recorded ACT ACETATE ION × 1 EDO 1,2-ETHANEDIOL × 5 H0N 5-[(3,4-dichlorophenyl)methyl]-4-oxidanylidene-1-piperidin-4-yl-~{N}-pyridin-4-yl-pyrazolo[4,3-c]pyridine-7-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；292 K；18-22% PEG 8000, 100-130 mM MgAc2, 100 mM citric acid pH 5.0
Resolution 1.49 Å R-free 0.195
7ZAU Fascin-1 in complex with Nb 3E11 Deposited 2022-03-22 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–493（493 aa）
Not recorded EDO 1,2-ETHANEDIOL × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.02 M D-glucose, D-mannose, D-galactose, L-fucose, D-xylose, N-acetyl-D-glucosamine; 0.1 M MES/imidazole pH 6.5, 10% PEG 8000, 20% ethylene glycol
Resolution 2.20 Å R-free 0.290
7ZAU Fascin-1 in complex with Nb 3E11 Deposited 2022-03-22 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 1–493（493 aa）
Not recorded EDO 1,2-ETHANEDIOL × 2 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.02 M D-glucose, D-mannose, D-galactose, L-fucose, D-xylose, N-acetyl-D-glucosamine; 0.1 M MES/imidazole pH 6.5, 10% PEG 8000, 20% ethylene glycol
Resolution 2.20 Å R-free 0.290
7ZAU Fascin-1 in complex with Nb 3E11 Deposited 2022-03-22 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 1–493（493 aa）
Not recorded EDO 1,2-ETHANEDIOL × 5 PEG DI(HYDROXYETHYL)ETHER × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.02 M D-glucose, D-mannose, D-galactose, L-fucose, D-xylose, N-acetyl-D-glucosamine; 0.1 M MES/imidazole pH 6.5, 10% PEG 8000, 20% ethylene glycol
Resolution 2.20 Å R-free 0.290
7ZAU Fascin-1 in complex with Nb 3E11 Deposited 2022-03-22 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain G 1–493（493 aa）
Not recorded EDO 1,2-ETHANEDIOL × 3 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；0.02 M D-glucose, D-mannose, D-galactose, L-fucose, D-xylose, N-acetyl-D-glucosamine; 0.1 M MES/imidazole pH 6.5, 10% PEG 8000, 20% ethylene glycol
Resolution 2.20 Å R-free 0.290
8VO5 Cryo-EM structure of fascin bound to F-actin (actin binding site 1) Deposited 2024-01-14 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–493（493 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
8VO6 Cryo-EM structure of fascin bound to F-actin (actin binding site 2) Deposited 2024-01-14 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–493（493 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
8VO7 Cryo-EM structure of fascin crosslinked F-actin Deposited 2024-01-14 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric
Chain A 1–493（493 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
8VO8 Cryo-EM structure of fascin crosslinked F-actin (Eigen_left) Deposited 2024-01-14 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric
Chain A 1–493（493 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 Å
8VO9 Cryo-EM structure of fascin crosslinked F-actin (Eigen_middle) Deposited 2024-01-14 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric
Chain A 1–493（493 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
8VOA Cryo-EM structure of fascin crosslinked F-actin (Eigen_right) Deposited 2024-01-14 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric
Chain A 1–493（493 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.00 Å
9FN6 Full-length crystal structure of human Fascin 1 Deposited 2024-06-09 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–493（493 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0,1M HEPES pH 7.5, 20% polyethylene glycol (PEG) 4000, 2% propanol
Resolution 2.20 Å R-free 0.304
9FN6 Full-length crystal structure of human Fascin 1 Deposited 2024-06-09 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–493（493 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0,1M HEPES pH 7.5, 20% polyethylene glycol (PEG) 4000, 2% propanol
Resolution 2.20 Å R-free 0.304
9GS6 Crystal structure of fascin in complex with compound 4 Deposited 2024-09-13 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–493（493 aa）
Not recorded ACT ACETATE ION × 1 A1IPD N-(1-(3,4-dichlorobenzyl)-6-oxo-1,6-dihydropyridin-3-yl)-5-oxopyrrolidine-2-carboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；292 K；18-22% PEG 8000, 100-130 mM MgAc2, 100 mM citric acid pH 5.0
Resolution 1.97 Å R-free 0.268
9GXI Subtomogram average of fascin-actin complex Deposited 2024-09-30 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric
Chain A 1–493（493 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 9.00 Å

27 other PDB entries and 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FSCN1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–493； UniProt 1–493 Author chain B； PDBConstruct 1–493； UniProt 1–493

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 4gp0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4gp0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4gp0
Deposition date deposition_date2012-08-20
Structure title titleThe crystal structure of human fascin 1 R149A K150A R151A mutant
Keywords keywordsbeta-trefoil, actin bundling protein, cancer, metastasis, cell migration, Actin-binding, Phosphoprotein, PROTEIN BINDING, Actin; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier33.30 Å
Radius of gyration Rg (electron density) rg_electron32.32 Å
Forward intensity I(0) i0205120000.00
Molecular weight molecular_weight109010.0 kDa
Excluded volume excluded_volume133830 ų
Envelope volume envelope_volume168690 ų
Hydration-shell volume shell_volume43344 ų
Envelope diameter envelope_diameter112.4 Å
Shell Rg shell_rg39.48 Å
Envelope Rg envelope_rg31.80 Å
Shape Rg shape_rg32.28 Å
Total Rg total_rg32.96 Å
Total atoms total_atoms7595
Residues n_residues960
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax107.4 Å
Rg (real space) rg_real33.18 Å
Rg uncertainty (real space) rg_real_error0.83 Å
I(0) (real space) i0_real2.0510e+08
I(0) uncertainty (real space) i0_real_error3.6840e+06
Rg (reciprocal space) rg_reciprocal33.23 Å
I(0) (reciprocal space) i0_reciprocal205100000.0000
Solution quality estimate total_estimate0.8993
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.5 Å
Skewness Skewness skewness0.214
Kurtosis Kurtosis kurtosis-0.485
Angular range angular_range— – 0.2400 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37640000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.936
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (7)

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7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd4gp0a1
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.5 — Actin-crosslinking proteins
Family Family familyb.42.5.1 — Fascin
Domain ID domain_idd4gp0a2
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.5 — Actin-crosslinking proteins
Family Family familyb.42.5.1 — Fascin
Domain ID domain_idd4gp0a3
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.5 — Actin-crosslinking proteins
Family Family familyb.42.5.1 — Fascin
Domain ID domain_idd4gp0a4
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.5 — Actin-crosslinking proteins
Family Family familyb.42.5.1 — Fascin
Domain ID domain_idd4gp0b1
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.5 — Actin-crosslinking proteins
Family Family familyb.42.5.1 — Fascin
Domain ID domain_idd4gp0b2
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.5 — Actin-crosslinking proteins
Family Family familyb.42.5.1 — Fascin
Domain ID domain_idd4gp0b3
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.5 — Actin-crosslinking proteins
Family Family familyb.42.5.1 — Fascin
Domain ID domain_idd4gp0b4
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.5 — Actin-crosslinking proteins
Family Family familyb.42.5.1 — Fascin

CATH v4.4 (8 domains)

Domain ID domain_id4gp0A01
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50 —
Domain ID domain_id4gp0A02
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50 —
Domain ID domain_id4gp0A03
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50 —
Domain ID domain_id4gp0A04
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50 —
Domain ID domain_id4gp0B01
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50 —
Domain ID domain_id4gp0B02
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50 —
Domain ID domain_id4gp0B03
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50 —
Domain ID domain_id4gp0B04
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50 —
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8. Citations (1)

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9. Files and Curves (10)