5UQ1: Human Cdk2-Spy1 complex

Crystal structure of human Cdk2-Spy1 complex. Determined by X-ray diffraction at 3.2 Å resolution. Released 5 Jul 2017.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: Homo sapiens
Chains: 4
Atoms: 6,913
Mol. weight: 107.24 kDa
Released: 5 Jul 2017

Explore 5UQ1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5UQ1 contains 55 α-helices and 22 β-strands across 4 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: 16 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	1
β-strand	16-20	5	1
β-strand	30-35	6	1
α-helix	36-38	3
α-helix	43-45	3
α-helix	46-55	10
β-strand	63	1	2
α-helix	64-65	2
β-strand	66-71	6	1
β-strand	76-81	6	1
β-strand	85-86	2	2
α-helix	87-93	7
α-helix	101-120	20
β-strand	123-124	2	3
α-helix	130-132	3
β-strand	133-135	3	2
β-strand	141-143	3	2
β-strand	150-151	2	3
α-helix	166-168	3
α-helix	171-174	4
α-helix	183-197	15
α-helix	208-219	12
α-helix	230-232	3
α-helix	244-246	3
α-helix	248-251	4
α-helix	259-266	8
α-helix	277-280	4

Chains B and D: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	72-75	4
α-helix	76-79	4
α-helix	81-89	9
α-helix	98-110	13
α-helix	115-117	3
α-helix	120-134	15
α-helix	140-143	4
α-helix	144-149	6
α-helix	153-155	3
α-helix	157-170	14
α-helix	179-185	7
α-helix	193-196	4

Chain C: 15 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	4
β-strand	16-23	8	4
β-strand	29-35	7	4
α-helix	36-38	3
α-helix	43-45	3
α-helix	46-55	10
β-strand	63	1	5
α-helix	64-65	2
β-strand	66-71	6	4
β-strand	76-81	6	4
β-strand	85-86	2	5
α-helix	88-93	6
α-helix	101-120	20
β-strand	123-124	2	6
α-helix	130-132	3
β-strand	133-135	3	5
β-strand	141-143	3	5
β-strand	150-151	2	6
α-helix	166-168	3
α-helix	171-174	4
α-helix	183-197	15
α-helix	208-219	12
α-helix	230-232	3
α-helix	244-246	3
α-helix	259-266	8
α-helix	277-281	5

Molecules and chains

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

Sequence of entity 1 (A, C), FASTA

>5UQ1_1 Cyclin-dependent kinase 2 (chains A, C)
GEFMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKE
LNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAF
CHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGC
KYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYK
PSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLR
L

Sequence of entity 2 (B, D), FASTA

>5UQ1_2 Speedy protein A (chains B, D)
GAMDPEFGPCLVIQRQDMTAFFKLFDDDLIQDFLWMDCCCKIADKYLLAMTFVYFKRAKF
TISEHTRINFFIALYLANTVEEDEEETKYEIFPWALGKNWRKLFPNFLKLRDQLWDRIDY
RAIVSRRCCEEVMAIAPTHYIWQRERSVHHSGAVRNYNRD

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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