5UQ3: Human Cdk2-Spy1-P27 ternary complex

Crystal structure of human Cdk2-Spy1-P27 ternary complex. Determined by X-ray diffraction at 3.6 Å resolution. Released 5 Jul 2017.

Method: X-ray diffraction
Resolution: 3.6 Å
Organism: Homo sapiens
Chains: 3
Atoms: 3,680
Mol. weight: 76.06 kDa
Released: 5 Jul 2017

Explore 5UQ3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5UQ3 contains 26 α-helices and 13 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: 14 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	30-31	2	1
β-strand	34	1	2
α-helix	46-55	10
β-strand	63	1	3
β-strand	66	1	1
β-strand	72	1	4
β-strand	75	1	4
β-strand	77	1	2
β-strand	80-81	2	1
β-strand	85-86	2	3
α-helix	87-91	5
α-helix	101-120	20
β-strand	124	1	5
α-helix	130-132	3
β-strand	133-135	3	3
β-strand	141-143	3	3
β-strand	150	1	5
α-helix	166-168	3
α-helix	171-174	4
α-helix	183-198	16
α-helix	211-218	8
α-helix	230-232	3
α-helix	240-242	3
α-helix	248-251	4
α-helix	257-266	10
α-helix	277-280	4
α-helix	284-288	5

Chain B: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	72-75	4
α-helix	76-79	4
α-helix	81-89	9
α-helix	100-110	11
α-helix	120-134	15
α-helix	140-144	5
α-helix	145-149	5
α-helix	158-170	13
α-helix	179-185	7
α-helix	193-196	4

Chain C: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	559-566	8
α-helix	587-589	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cyclin-dependent kinase 2	A	protein	301	Homo sapiens	P24941 (AlphaFold model)
Speedy protein A	B	protein	160	Homo sapiens	Q5MJ70 (AlphaFold model)
Cyclin-dependent kinase inhibitor 1B	C	protein	201	Homo sapiens	P46527 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5UQ3_1 Cyclin-dependent kinase 2 (chains A)
GEFMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKE
LNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAF
CHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGC
KYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYK
PSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLR
L

Sequence of entity 2 (B), FASTA

>5UQ3_2 Speedy protein A (chains B)
GAMDPEFGPCLVIQRQDMTAFFKLFDDDLIQDFLWMDCCCKIADKYLLAMTFVYFKRAKF
TISEHTRINFFIALYLANTVEEDEEETKYEIFPWALGKNWRKLFPNFLKLRDQLWDRIDY
RAIVSRRCCEEVMAIAPTHYIWQRERSVHHSGAVRNYNRD

Sequence of entity 3 (C), FASTA

>5UQ3_3 Cyclin-dependent kinase inhibitor 1B (chains C)
GEFMSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQ
RKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDVSGSRPAAP
LIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATDDSSTQNKRANRTEENVSDG
SPNAGSVEQTPKKPGLRRRQT

Primary citation

Structural basis of divergent cyclin-dependent kinase activation by Spy1/RINGO proteins. McGrath, D.A., Fifield, B.A., Marceau, A.H. et al. EMBO J (2017) 36:2251-2262. DOI 10.15252/embj.201796905 · PubMed

Other PDB entries of the same protein (UniProt P24941 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6Q4G 0.98 Å, CDK2 in complex with FragLite37
6Q49 1.0 Å, CDK2 in complex with FragLite6
6Q4H 1.0 Å, CDK2 in complex with FragLite36
6Q48 1.03 Å, CDK2 in complex with FragLite7
6Q4J 1.05 Å, CDK2 in complex with FragLite34
6Q4E 1.06 Å, CDK2 in complex with FragLite33
6Q4K 1.06 Å, CDK2 in complex with FragLite38
6Q4D 1.07 Å, CDK2 in complex with FragLite31
6Q3B 1.11 Å, CDK2 in complex with FragLite2
6Q4I 1.11 Å, CDK2 in complex with FragLite35
6Q4B 1.12 Å, CDK2 in complex with FragLite13
6Q4A 1.13 Å, CDK2 in complex with FragLite14

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