1FIN: Cyclin a-cyclin-dependent kinase 2 complex

Cyclin a-cyclin-dependent kinase 2 complex. Determined by X-ray diffraction at 2.3 Å resolution. Released 27 Jan 1997.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 4
Atoms: 9,476
Mol. weight: 128.7 kDa
Ligands: ATP
Released: 27 Jan 1997

Explore 1FIN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1FIN contains 73 α-helices and 32 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: 18 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	1
β-strand	17-23	7	1
β-strand	29-35	7	1
β-strand	38	1	2
β-strand	43	1	2
α-helix	46-55	10
β-strand	63	1	3
α-helix	64-65	2
β-strand	66-71	6	1
β-strand	76-81	6	1
β-strand	85-86	2	3
α-helix	87-93	7
α-helix	101-120	20
β-strand	123-124	2	4
α-helix	130-132	3
β-strand	133-135	3	3
β-strand	141-143	3	3
α-helix	146-148	3
β-strand	150-151	2	4
α-helix	156	1
β-strand	157	1	5
α-helix	158	1
β-strand	159	1	6
β-strand	162	1	6
α-helix	166-168	3
α-helix	171-174	4
β-strand	179	1	5
α-helix	182-198	17
α-helix	208-219	12
α-helix	230-232	3
α-helix	245-247	3
α-helix	248-251	4
α-helix	257-266	10
α-helix	277-280	4
α-helix	284-286	3

Chain B: 20 helices, 0 β-strands

Element	Residues	Length
α-helix	176-178	3
α-helix	179-193	15
α-helix	208-225	18
α-helix	229-242	14
α-helix	250-252	3
α-helix	253-268	16
α-helix	272-274	3
α-helix	275-280	6
α-helix	288-302	15
α-helix	311-319	9
α-helix	327-340	14
α-helix	344-347	4
α-helix	352-368	17
α-helix	374-380	7
α-helix	384-399	16
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 C: 16 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	7
β-strand	18-23	6	7
β-strand	29-35	7	7
β-strand	38	1	8
β-strand	43	1	8
α-helix	46-55	10
β-strand	63	1	9
β-strand	66-71	6	7
β-strand	76-81	6	7
β-strand	85-86	2	9
α-helix	87-92	6
α-helix	101-120	20
β-strand	123-124	2	10
α-helix	130-132	3
β-strand	133-135	3	9
β-strand	141-143	3	9
β-strand	150-151	2	10
α-helix	156	1
β-strand	157	1	11
α-helix	158	1
α-helix	163-165	3
α-helix	166-168	3
α-helix	171-174	4
β-strand	179	1	11
α-helix	182-198	17
α-helix	208-219	12
α-helix	230-232	3
α-helix	248-251	4
α-helix	257-266	10
α-helix	277-282	6
α-helix	284-288	5

Chain D: 19 helices, 0 β-strands

Element	Residues	Length
α-helix	175-190	16
α-helix	194-196	3
α-helix	208-225	18
α-helix	229-243	15
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	352-367	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

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cyclin-dependent kinase 2	A, C	protein	298	Homo sapiens	P24941 (AlphaFold model)
Cyclin a	B, D	protein	260	Homo sapiens	P20248 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1FIN_1 CYCLIN-DEPENDENT KINASE 2 (chains A, C)
MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNH
PNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS
HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYY
STAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF
PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL

Sequence of entity 2 (B, D), FASTA

>1FIN_2 CYCLIN A (chains B, D)
NEVPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDWLVEVGEEYKLQNETL
HLAVNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVL
RMEHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMFLGELSLIDADPYLKYLP
SVIAGAAFHLALYTVTGQSWPESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREK
YKNSKYHGVSLLNPPETLNL

Ligands and cofactors

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

Primary citation

Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Jeffrey, P.D., Russo, A.A., Polyak, K. et al. Nature (1995) 376:313-320. DOI 10.1038/376313a0 · 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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1FIN is part of these collections:

Kinases and cancer drug targets

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