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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：Q15078 New Search
11PDB entries
22Biological assembly
22chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion 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
1H4L Structure and regulation of the CDK5-p25(nck5a) complex Deposited 2001-05-11 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain D 147–293（147 aa） Fragment：RESIDUES 147-293
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；293 K；MICROSEEDING - PEG3350, 100 MM TRIS PH 7.6, 200 MM KI, 10 MM DTT, PROTEIN CONC.:7 MG/ML HANGING DROP 2+2 UL. TEMPERATURE 293K.
Resolution 2.65 Å R-free 0.287
1H4L Structure and regulation of the CDK5-p25(nck5a) complex Deposited 2001-05-11 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain E 147–293（147 aa） Fragment：RESIDUES 147-293
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；293 K；MICROSEEDING - PEG3350, 100 MM TRIS PH 7.6, 200 MM KI, 10 MM DTT, PROTEIN CONC.:7 MG/ML HANGING DROP 2+2 UL. TEMPERATURE 293K.
Resolution 2.65 Å R-free 0.287
1UNG Structural mechanism for the inhibition of CDK5-p25 by roscovitine, aloisine and indirubin. Deposited 2003-09-10 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain D 100–307（208 aa） Fragment：RESIDUES 100-307
Not recorded ALH 6-PHENYL[5H]PYRROLO[2,3-B]PYRAZINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；13% PEG 3350, 0.1M KI, 0.1M BISTRISPROPANE PH 7.0, 10MM DTT
Resolution 2.30 Å R-free 0.225
1UNG Structural mechanism for the inhibition of CDK5-p25 by roscovitine, aloisine and indirubin. Deposited 2003-09-10 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain E 100–307（208 aa） Fragment：RESIDUES 100-307
Not recorded ALH 6-PHENYL[5H]PYRROLO[2,3-B]PYRAZINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；13% PEG 3350, 0.1M KI, 0.1M BISTRISPROPANE PH 7.0, 10MM DTT
Resolution 2.30 Å R-free 0.225
1UNH Structural mechanism for the inhibition of CDK5-p25 by roscovitine, aloisine and indirubin. Deposited 2003-09-10 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain D 100–307（208 aa） Fragment：RESIDUES 100-307
Not recorded IXM (Z)-1H,1'H-[2,3']BIINDOLYLIDENE-3,2'-DIONE-3-OXIME × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；13% PEG 3350, 0.1 M KI 0.1 M BISTRISPROPANE PH 7.0, 10 MM DTT
Resolution 2.35 Å R-free 0.230
1UNH Structural mechanism for the inhibition of CDK5-p25 by roscovitine, aloisine and indirubin. Deposited 2003-09-10 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain E 100–307（208 aa） Fragment：RESIDUES 100-307
Not recorded IXM (Z)-1H,1'H-[2,3']BIINDOLYLIDENE-3,2'-DIONE-3-OXIME × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；13% PEG 3350, 0.1 M KI 0.1 M BISTRISPROPANE PH 7.0, 10 MM DTT
Resolution 2.35 Å R-free 0.230
1UNL Structural mechanism for the inhibition of CD5-p25 from the roscovitine, aloisine and indirubin. Deposited 2003-09-10 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain D 100–307（208 aa） Fragment：RESIDUES 100-307
Mutation：YES RRC R-ROSCOVITINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；13% PEG 3350, 0.1 M KI, 0.1 M BISTRISPROPANE PH 7.0, 10 MM DTT
Resolution 2.20 Å R-free 0.219
1UNL Structural mechanism for the inhibition of CD5-p25 from the roscovitine, aloisine and indirubin. Deposited 2003-09-10 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain E 100–307（208 aa） Fragment：RESIDUES 100-307
Mutation：YES No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；13% PEG 3350, 0.1 M KI, 0.1 M BISTRISPROPANE PH 7.0, 10 MM DTT
Resolution 2.20 Å R-free 0.219
3O0G Crystal Structure of Cdk5:p25 in complex with an ATP analogue Deposited 2010-07-19 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain D 145–293（149 aa） Fragment：UNP residues 146-293
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；293 K；PEG 3350, KI, Bis-Tris Propane, pH 7, vapor diffusion, temperature 293K
Resolution 1.95 Å R-free 0.256
3O0G Crystal Structure of Cdk5:p25 in complex with an ATP analogue Deposited 2010-07-19 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain E 145–293（149 aa） Fragment：UNP residues 146-293
Not recorded 3O0 {4-amino-2-[(4-chlorophenyl)amino]-1,3-thiazol-5-yl}(3-nitrophenyl)methanone × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；293 K；PEG 3350, KI, Bis-Tris Propane, pH 7, vapor diffusion, temperature 293K
Resolution 1.95 Å R-free 0.256
6LDP Structure of CDK5R1-bound FEM1C Deposited 2019-11-22 Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 298–307（10 aa）
Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.2M Lithium sulfate, 0.1M Tris-Hcl pH 7.9
Resolution 2.35 Å R-free 0.258
6LDP Structure of CDK5R1-bound FEM1C Deposited 2019-11-22 Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 298–307（10 aa）
Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.2M Lithium sulfate, 0.1M Tris-Hcl pH 7.9
Resolution 2.35 Å R-free 0.258
7CNG Structure of CDK5R1 bound FEM1B Deposited 2020-07-31 Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 298–307（10 aa）
Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；1.6M Magnesium sulfate hydrate, 0.1M BIS-TRIS propane pH 6.7
Resolution 3.49 Å R-free 0.267
7CNG Structure of CDK5R1 bound FEM1B Deposited 2020-07-31 Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 298–307（10 aa）
Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；1.6M Magnesium sulfate hydrate, 0.1M BIS-TRIS propane pH 6.7
Resolution 3.49 Å R-free 0.267
7VDP The structure of cyclin-dependent kinase 5 (CDK5) in complex with p25 and Compound 1 Deposited 2021-09-07 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain C 100–307（208 aa）
Not recorded 65L [1-[3-fluoranyl-4-[(2-piperidin-4-yloxy-1,6-naphthyridin-7-yl)amino]phenyl]pyrazol-3-yl]methanol × 1 EDO 1,2-ETHANEDIOL × 10 PEG DI(HYDROXYETHYL)ETHER × 2 CL CHLORIDE ION × 7 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；291 K；0.1M MES pH 5.5, 0.3M MgCl2, 20% PEG3350
Resolution 2.09 Å R-free 0.229
7VDP The structure of cyclin-dependent kinase 5 (CDK5) in complex with p25 and Compound 1 Deposited 2021-09-07 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain D 100–307（208 aa）
Not recorded 65L [1-[3-fluoranyl-4-[(2-piperidin-4-yloxy-1,6-naphthyridin-7-yl)amino]phenyl]pyrazol-3-yl]methanol × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；291 K；0.1M MES pH 5.5, 0.3M MgCl2, 20% PEG3350
Resolution 2.09 Å R-free 0.229
7VDQ The structure of cyclin-dependent kinase 5 (CDK5) in complex with p25 and Compound 7 Deposited 2021-09-07 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain C 100–307（208 aa）
Not recorded 64V 2-[[7-[[2-fluoranyl-4-[3-(hydroxymethyl)pyrazol-1-yl]phenyl]amino]-1,6-naphthyridin-2-yl]-(1-methylpiperidin-4-yl)amino]ethanoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；291 K；0.1M MES pH 5.5, 0.3M MgCl2, 20% PEG3350
Resolution 2.91 Å R-free 0.284
7VDQ The structure of cyclin-dependent kinase 5 (CDK5) in complex with p25 and Compound 7 Deposited 2021-09-07 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain D 100–307（208 aa）
Not recorded 64V 2-[[7-[[2-fluoranyl-4-[3-(hydroxymethyl)pyrazol-1-yl]phenyl]amino]-1,6-naphthyridin-2-yl]-(1-methylpiperidin-4-yl)amino]ethanoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；291 K；0.1M MES pH 5.5, 0.3M MgCl2, 20% PEG3350
Resolution 2.91 Å R-free 0.284
7VDR The structure of cyclin-dependent kinase 5 (CDK5) in complex with p25 and Compound 13 Deposited 2021-09-07 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain C 100–307（208 aa）
Not recorded 63I (1R)-1-[7-[(2-fluoranyl-4-pyrazol-1-yl-phenyl)amino]-1,6-naphthyridin-2-yl]-1-(1-methylpiperidin-4-yl)ethanol × 1 PGE TRIETHYLENE GLYCOL × 1 EDO 1,2-ETHANEDIOL × 9 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 5.5；291 K；0.1M MES pH 5.5, 0.3M MgCl2, 20% PEG3350
Resolution 2.55 Å R-free 0.256
7VDR The structure of cyclin-dependent kinase 5 (CDK5) in complex with p25 and Compound 13 Deposited 2021-09-07 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain D 100–307（208 aa）
Not recorded 63I (1R)-1-[7-[(2-fluoranyl-4-pyrazol-1-yl-phenyl)amino]-1,6-naphthyridin-2-yl]-1-(1-methylpiperidin-4-yl)ethanol × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 5.5；291 K；0.1M MES pH 5.5, 0.3M MgCl2, 20% PEG3350
Resolution 2.55 Å R-free 0.256
7VDS The structure of cyclin-dependent kinase 5 (CDK5) in complex with p25 and Compound 24 Deposited 2021-09-07 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain C 100–307（208 aa）
Not recorded 61U 5-fluoranyl-4-[[2-[(1R)-1-(1-methylpiperidin-4-yl)-1-oxidanyl-ethyl]-1,6-naphthyridin-7-yl]amino]-2-morpholin-4-yl-benzenecarbonitrile × 1 GOL GLYCEROL × 8 EDO 1,2-ETHANEDIOL × 17 CL CHLORIDE ION × 19 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；291 K；0.1M MES pH 5.5, 0.3M MgCl2, 20% PEG3350
Resolution 3.05 Å R-free 0.272
7VDS The structure of cyclin-dependent kinase 5 (CDK5) in complex with p25 and Compound 24 Deposited 2021-09-07 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain D 100–307（208 aa）
Not recorded EDO 1,2-ETHANEDIOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；291 K；0.1M MES pH 5.5, 0.3M MgCl2, 20% PEG3350
Resolution 3.05 Å R-free 0.272

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.