6P3W: Cyclin A-CDK2-ORC1 complex

Crystal structure of the Cyclin A-CDK2-ORC1 complex. Determined by X-ray diffraction at 2.54 Å resolution. Released 31 Jul 2019.

Method: X-ray diffraction
Resolution: 2.54 Å
Organism: Homo sapiens
Chains: 6
Atoms: 8,967
Mol. weight: 129.92 kDa
Ligands: PO4
Released: 31 Jul 2019

Explore 6P3W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6P3W contains 76 α-helices and 29 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, 15 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	1
β-strand	17-23	7	1
β-strand	29-36	8	1
α-helix	46-55	10
β-strand	63	1	2
β-strand	66-71	6	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	155-156	2
β-strand	157	1	4
α-helix	158	1
β-strand	159	1	5
β-strand	162	1	5
α-helix	166-168	3
α-helix	171-174	4
β-strand	179	1	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	271-273	3
α-helix	275-276	2
α-helix	277-281	5
α-helix	284-286	3

Chain B: 19 helices, 0 β-strands

Element	Residues	Length
α-helix	178-192	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	388-399	12
α-helix	401-403	3
α-helix	408-412	5
α-helix	416-418	3
α-helix	421-423	3

Chain C: 17 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	6
β-strand	17-23	7	6
β-strand	29-36	8	6
α-helix	46-55	10
β-strand	60	1	7
β-strand	63	1	7
β-strand	66-71	6	6
β-strand	75-81	7	6
β-strand	85-86	2	7
α-helix	87-93	7
α-helix	101-120	20
β-strand	123-124	2	8
α-helix	130-132	3
β-strand	133-135	3	7
β-strand	141-143	3	7
β-strand	150-151	2	8
α-helix	155-156	2
β-strand	157	1	9
α-helix	158	1
α-helix	166-168	3
α-helix	171-174	4
β-strand	179	1	9
α-helix	182-198	17
α-helix	208-219	12
α-helix	230-232	3
α-helix	244-247	4
α-helix	248-251	4
α-helix	257-266	10
α-helix	275-276	2
α-helix	277-281	5
α-helix	284-288	5

Chain D: 22 helices, 0 β-strands

Element	Residues	Length
α-helix	178-192	15
α-helix	194-196	3
α-helix	199-202	4
α-helix	208-224	17
α-helix	229-242	14
α-helix	250-252	3
α-helix	253-268	16
α-helix	272-274	3
α-helix	275-281	7
α-helix	288-302	15
α-helix	311-318	8
α-helix	319-321	3
α-helix	327-339	13
α-helix	344-347	4
α-helix	352-367	16
α-helix	374-380	7
α-helix	388-400	13
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-A2	B, D	protein	257	Homo sapiens	P20248 (AlphaFold model)
ORC1 Peptide	E, F	protein	7	Homo sapiens	Q13415 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>6P3W_1 Cyclin-dependent kinase 2 (chains A, C)
MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNH
PNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS
HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYY
STAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF
PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL

Sequence of entity 2 (B, D), FASTA

>6P3W_2 Cyclin-A2 (chains B, D)
PDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDWLVEVGEEYKLQNETLHLA
VNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRME
HLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMFLGELSLIDADPYLKYLPSVI
AGAAFHLALYTVTGQSWPESLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKN
SKYHGVSLLNPPETLNL

Sequence of entity 3 (E, F), FASTA

>6P3W_3 ORC1 Peptide (chains E, F)
ARKRLEL

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	12

Primary citation

Structural basis for the ORC1-Cyclin A association. Wang, B., Song, J. Protein Sci (2019) 28:1727-1733. DOI 10.1002/pro.3689 · 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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