3UVU: Nuclear import of Flap endonuclease 1

Structural basis of nuclear import of Flap endonuclease 1 (FEN1). Determined by X-ray diffraction at 2.38 Å resolution. Released 27 Jun 2012.

Method: X-ray diffraction
Resolution: 2.38 Å
Organisms: Homo sapiens, Mus musculus
Chains: 2
Atoms: 3,477
Mol. weight: 57.44 kDa
Released: 27 Jun 2012

Explore 3UVU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3UVU contains 32 α-helices and 0 β-strands across 1 chain. 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: 32 helices, 0 β-strands

Element	Residues	Length
α-helix	78-85	8
α-helix	90-104	15
α-helix	112-117	6
α-helix	121-127	7
α-helix	134-148	15
α-helix	152-160	9
α-helix	163-169	7
α-helix	170-172	3
α-helix	176-190	15
α-helix	194-202	9
α-helix	206-211	6
α-helix	218-220	3
α-helix	223-236	14
α-helix	243-245	3
α-helix	246-259	14
α-helix	265-278	14
α-helix	283-290	8
α-helix	295-302	8
α-helix	307-320	14
α-helix	325-333	9
α-helix	336-339	4
α-helix	340-343	4
α-helix	349-363	15
α-helix	367-375	9
α-helix	378-387	10
α-helix	391-407	17
α-helix	410-418	9
α-helix	422-428	7
α-helix	434-452	19
α-helix	457-466	10
α-helix	469-474	6
α-helix	482-495	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Flap endonuclease 1 (Fen1) peptide	B	protein	19	Homo sapiens	P39748 (AlphaFold model)
Importin subunit alpha-2	A	protein	510	Mus musculus	P52293 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>3UVU_1 Flap endonuclease 1 (Fen1) peptide (chains B)
SAKRKEPEPKGSTKKKAKT

Sequence of entity 2 (A), FASTA

>3UVU_2 Importin subunit alpha-2 (chains A)
MHHHHHHSSGLVPRGSGMKETAAAKFERQHMDSPDLGTDDDDKAMADIGSNQGTVNWSVE
DIVKGINSNNLESQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLGKTDCSPIQFE
SAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNIAGDGSAFRDL
VIKHGAIDPLLALLAVPDLSTLACGYLRNLTWTLSNLCRNKNPAPPLDAVEQILPTLVRL
LHHNDPEVLADSCWAISYLTDGPNERIEMVVKKGVVPQLVKLLGATELPIVTPALRAIGN
IVTGTDEQTQKVIDAGALAVFPSLLTNPKTNIQKEATWTMSNITAGRQDQIQQVVNHGLV
PFLVGVLSKADFKTQKEAAWAITNYTSGGTVEQIVYLVHCGIIEPLMNLLSAKDTKIIQV
ILDAISNIFQAAEKLGETEKLSIMIEECGGLDKIEALQRHENESVYKASLNLIEKYFSVE
EEEDQNVVPETTSEGFAFQVQDGAPGTFNF

Primary citation

Structural basis of nuclear import of flap endonuclease 1 (FEN1). de Barros, A.C., Takeda, A.A., Chang, C.W. et al. Acta Crystallogr D Biol Crystallogr (2012) 68:743-750. DOI 10.1107/S0907444912010281 · PubMed

Other PDB entries of the same protein (UniProt P39748 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9RCI 1.66 Å, Crystal Structure of Flap Endonuclease FEN1 with Compound 28
1U7B 1.88 Å, Crystal structure of hPCNA bound to residues 331-350 of the flap endonuclease-1 (FEN1)
5ZOD 1.9 Å, Crystal Structure of hFen1 in apo form
5ZOE 1.95 Å, Crystal Structure of D181A hFen1 in complex with DNA
5E0V 2.07 Å, Human PCNA variant (S228I) complexed with FEN1 at 2.1 Angstroms
5K97 2.1 Å, Flap endonuclease 1 (FEN1) D233N with cleaved product fragment and Sm3+
5KSE 2.1 Å, Flap endonuclease 1 (FEN1) R100A with 5'-flap substrate DNA and Sm3+
9RDI 2.1 Å, Crystal Structure of Flap Endonuclease FEN1 with Compound 5
3Q8K 2.2 Å, Crystal Structure of Human Flap Endonuclease FEN1 (WT) in complex with product 5'-flap…
5ZOF 2.25 Å, Crystal Structure of D181A/R192F hFen1 in complex with DNA
5ZOG 2.3 Å, Crystal Structure of R192F hFen1 in complex with DNA
3Q8L 2.32 Å, Crystal Structure of Human Flap Endonuclease FEN1 (WT) in complex with substrate 5'-flap…

Browse structure collections

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