2CCH: CDK2 cyclin A

The crystal structure of CDK2 cyclin A in complex with a substrate peptide derived from CDC modified with a gamma-linked ATP analogue. Determined by X-ray diffraction at 1.7 Å resolution. Released 3 May 2006.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: HOMO SAPIENS
Chains: 6
Atoms: 10,526
Mol. weight: 132.24 kDa
Ligands: ATP
Released: 3 May 2006

Explore 2CCH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2CCH contains 77 α-helices and 22 β-strands across 5 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	4-13	10	1
β-strand	16-23	8	1
β-strand	29-36	8	1
α-helix	46-55	10
β-strand	63	1	2
α-helix	64-65	2
β-strand	66-72	7	1
β-strand	75-81	7	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	183-198	16
α-helix	208-219	12
α-helix	230-232	3
α-helix	248-250	3
α-helix	257-266	10
α-helix	275-276	2
α-helix	277-280	4
α-helix	284-286	3
α-helix	292-294	3

Chain B: 20 helices, 0 β-strands

Element	Residues	Length
α-helix	179-193	15
α-helix	194-196	3
α-helix	199-202	4
α-helix	208-224	17
α-helix	229-245	17
α-helix	250-268	19
α-helix	272-274	3
α-helix	275-281	7
α-helix	288-301	14
α-helix	311-319	9
α-helix	327-342	16
α-helix	344-347	4
α-helix	352-368	17
α-helix	374-380	7
α-helix	384-400	17
α-helix	401-403	3
α-helix	408-413	6
α-helix	416-418	3
α-helix	421-423	3
α-helix	425-427	3

Chain C: 19 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	4-13	10	4
β-strand	16-23	8	4
β-strand	29-36	8	4
α-helix	46-55	10
β-strand	63	1	5
α-helix	64-65	2
β-strand	66-72	7	4
β-strand	75-81	7	4
β-strand	85-86	2	5
α-helix	87-93	7
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
α-helix	146-148	3
β-strand	150-151	2	6
α-helix	156-158	3
α-helix	166-168	3
α-helix	171-174	4
α-helix	183-198	16
α-helix	208-219	12
α-helix	230-232	3
α-helix	243-247	5
α-helix	248-251	4
α-helix	257-266	10
α-helix	275-276	2
α-helix	277-281	5
α-helix	284-286	3
α-helix	292-295	4

Chain D: 21 helices, 0 β-strands

Element	Residues	Length
α-helix	179-192	14
α-helix	194-196	3
α-helix	199-202	4
α-helix	208-224	17
α-helix	229-245	17
α-helix	250-268	19
α-helix	272-274	3
α-helix	275-280	6
α-helix	288-301	14
α-helix	311-318	8
α-helix	319-321	3
α-helix	327-342	16
α-helix	344-347	4
α-helix	352-367	16
α-helix	374-380	7
α-helix	384-400	17
α-helix	401-403	3
α-helix	408-412	5
α-helix	416-418	3
α-helix	421-423	3
α-helix	425-427	3

Chain E: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	4-5	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cell division protein kinase 2	A, C	protein	299	HOMO SAPIENS	P24941 (AlphaFold model)
Cyclin A2	B, D	protein	260	HOMO SAPIENS	P20248 (AlphaFold model)
Cell division control protein 6 homolog	E, F	protein	12	HOMO SAPIENS	Q99741 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>2CCH_1 CELL DIVISION PROTEIN KINASE 2 (chains A, C)
SMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELN
HPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCH
SHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKY
YSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPS
FPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL

Sequence of entity 2 (B, D), FASTA

>2CCH_2 CYCLIN A2 (chains B, D)
NEVPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDWLVEVGEEYKLQNETL
HLAVNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVL
RMEHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMFLGELSLIDADPYLKYLP
SVIAGAAFHLALYTVTGQSWPESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREK
YKNSKYHGVSLLNPPETLNL

Sequence of entity 3 (E, F), FASTA

>2CCH_3 CELL DIVISION CONTROL PROTEIN 6 HOMOLOG (chains E, F)
HTLKGRRLVFDN

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2

Water and common crystallization additives (GOL, SO4) are not listed.

Primary citation

The Role of the Phospho-Cdk2/Cyclin a Recruitment Site in Substrate Recognition. Cheng, K.Y., Noble, M.E.M., Skamnaki, V. et al. J Biol Chem (2006) 281:23167. DOI 10.1074/JBC.M600480200 · 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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