6P8F: CDK4

Crystal structure of CDK4 in complex with CyclinD1 and P27. Determined by X-ray diffraction at 2.89 Å resolution. Released 25 Dec 2019.

Method: X-ray diffraction
Resolution: 2.89 Å
Organism: Homo sapiens
Chains: 3
Atoms: 4,498
Mol. weight: 72.19 kDa
Released: 25 Dec 2019

Explore 6P8F in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6P8F contains 30 α-helices and 11 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 17 helices, 0 β-strands

Element	Residues	Length
α-helix	26-34	9
α-helix	44-47	4
α-helix	54-70	17
α-helix	77-89	13
α-helix	96-98	3
α-helix	99-114	16
α-helix	118-120	3
α-helix	121-127	7
α-helix	134-147	14
α-helix	154-156	3
α-helix	157-165	9
α-helix	172-189	18
α-helix	193-195	3
α-helix	200-212	13
α-helix	214-216	3
α-helix	226-236	11
α-helix	241-262	22

Chain B: 12 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	21-24	4	1
β-strand	31-39	9	1
α-helix	48-60	13
β-strand	68	1	2
α-helix	69-70	2
β-strand	71-77	7	1
β-strand	84-91	8	1
β-strand	96	1	2
α-helix	97-102	6
α-helix	111-130	20
β-strand	143-145	3	2
β-strand	151-153	3	2
α-helix	180-183	4
α-helix	191-206	16
α-helix	216-227	12
α-helix	243-245	3
α-helix	263-272	10
α-helix	281-282	2
α-helix	283-287	5
α-helix	290-292	3

Chain C: 1 helix, 3 β-strands

Element	Residues	Length	Sheet
α-helix	38-60	23
β-strand	62-63	2	3
β-strand	68-69	2	3
β-strand	75-76	2	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
G1/S-specific cyclin-D1	A	protein	249	Homo sapiens	P24385 (AlphaFold model)
Cyclin-dependent kinase 4	B	protein	302	Homo sapiens	P11802 (AlphaFold model)
Cyclin-dependent kinase inhibitor 1B	C	protein	82	Homo sapiens	P46527 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6P8F_1 G1/S-specific cyclin-D1 (chains A)
DANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEVLPSMRKIVATWMLEVCEEQKCEEEVF
PLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELL
QMELLLVNKLKWNLAAMTPHDFIEHFLSKMPEAEENKQIIRKHAQTFVALCATDVKFISN
PPSMVAAGSVVAAVQGLNLRSPNNFLSYYRLTRFLSRVIKCDPDCLRACQEQIEALLESS
LRQAQQNMD

Sequence of entity 2 (B), FASTA

>6P8F_2 Cyclin-dependent kinase 4 (chains B)
GEFATSRYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVPNGEEGLPISTVREVALLR
RLEAFEHPNVVRLMDVCATSRTDREIKVTLVFEHVDQDLRTYLDKAPPPGLPAETIKDLM
RQFLRGLDFLHANCIVHRDLKPENILVTSGGTVKLADFGLARIYSYQMALTPVVVTLWYR
APEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDWPRD
VSLPRGAFPPRGPRPVQSVVPEMEESGAQLLLEMLTFNPHKRISAFRALQHSYLHKDEGN
PE

Sequence of entity 3 (C), FASTA

>6P8F_3 Cyclin-dependent kinase inhibitor 1B (chains C)
GEFKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEK
GSLPEFYYRPPKGACKVPAQES

Primary citation

p27 allosterically activates cyclin-dependent kinase 4 and antagonizes palbociclib inhibition. Guiley, K.Z., Stevenson, J.W., Lou, K. et al. Science (2019) 366. DOI 10.1126/science.aaw2106 · PubMed

Other PDB entries of the same protein (UniProt P24385 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9CSK 2.25 Å, Crystal structure of CDK4 cyclin D1 in complex with atirmociclib
2W96 2.3 Å, Crystal Structure of CDK4 in complex with a D-type cyclin
6P8E 2.3 Å, Crystal structure of CDK4 in complex with CyclinD1 and P27
2W9Z 2.45 Å, Crystal Structure of CDK4 in complex with a D-type cyclin
5VZU 2.7 Å, Crystal structure of the Skp1-FBXO31-cyclin D1 complex
2W99 2.8 Å, Crystal Structure of CDK4 in complex with a D-type cyclin
6P8G 2.8 Å, Crystal structure of CDK4 in complex with CyclinD1 and P27
2W9F 2.85 Å, Crystal Structure of CDK4 in complex with a D-type cyclin
6P8H 3.19 Å, Crystal structure of CDK4 in complex with CyclinD1 and P21
9IVD 3.55 Å, Cryo-EM structure of CyclinD1 bound AMBRA1-DDB1

Browse structure collections

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