5ZOD: HFen1 in apo form

Crystal Structure of hFen1 in apo form. Determined by X-ray diffraction at 1.9 Å resolution. Released 30 Jan 2019.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,204
Mol. weight: 37.87 kDa
Ligands: MG
Released: 30 Jan 2019

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

Secondary structure: helices and β-sheets

5ZOD contains 19 α-helices and 9 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: 19 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	1
α-helix	6-13	8
α-helix	15-17	3
β-strand	18-21	4	2
α-helix	23-26	4
β-strand	30-34	5	2
α-helix	64-76	13
β-strand	80-85	6	2
α-helix	89-90	2
α-helix	139-148	10
β-strand	152-154	3	2
α-helix	159-168	10
β-strand	174-176	3	2
α-helix	181-184	4
β-strand	189-192	4	2
α-helix	198-200	3
α-helix	202-203	2
β-strand	204-208	5	2
α-helix	209-216	8
α-helix	220-230	11
β-strand	232	1	1
α-helix	243-253	11
α-helix	256-262	7
α-helix	269-271	3
α-helix	276-284	9
α-helix	303-307	5
α-helix	308-313	6
α-helix	318-330	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Flap endonuclease 1	A	protein	333	Homo sapiens	P39748 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5ZOD_1 Flap endonuclease 1 (chains A)
MGIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGET
TSHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAE
QEVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDM
DCLTFGSPVLMRHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRG
IGPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSE
PNEEELIKFMCGEKQFSEERIRSGVKRLSKSRQ

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2

Water and common crystallization additives (K) are not listed.

Primary citation

Structural basis of 5' flap recognition and protein-protein interactions of human flap endonuclease 1. Xu, H., Shi, R., Han, W. et al. Nucleic Acids Res (2018) 46:11315-11325. DOI 10.1093/nar/gky911 · 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)
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…
3UVU 2.38 Å, Structural basis of nuclear import of Flap endonuclease 1 (FEN1)

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