1UL1: Human FEN1-PCNA complex

Crystal structure of the human FEN1-PCNA complex. Determined by X-ray diffraction at 2.9 Å resolution. Released 1 Mar 2005.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Homo sapiens
Chains: 6
Atoms: 13,162
Mol. weight: 214.07 kDa
Ligands: MG
Released: 1 Mar 2005

Explore 1UL1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1UL1 contains 81 α-helices and 93 β-strands across 6 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: 11 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	11
α-helix	10-17	8
β-strand	25-30	6	12
β-strand	34-40	7	12
β-strand	46-53	8	12
α-helix	54-56	3
β-strand	59-62	4	11
β-strand	66-71	6	12
α-helix	72-79	8
β-strand	87-92	6	11
β-strand	98-104	7	11
β-strand	110-117	8	11
α-helix	118	1
β-strand	119	1	12
β-strand	122-127	6	3
α-helix	128-130	3
β-strand	136-140	5	12
α-helix	141-154	14
β-strand	157-162	6	13
β-strand	166-173	8	13
β-strand	176-183	8	13
α-helix	184-185	2
β-strand	196-197	2	12
β-strand	203-208	6	13
α-helix	209-215	7
α-helix	216-221	6
β-strand	224-228	5	12
β-strand	235-241	7	12
β-strand	245-251	7	12
α-helix	252-253	2
β-strand	254	1	2
α-helix	255	1

Chain B: 5 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	14
α-helix	10-20	11
β-strand	26-30	5	15
β-strand	34-40	7	15
β-strand	46-53	8	15
β-strand	59	1	14
β-strand	66-70	5	15
α-helix	72-79	8
β-strand	87-92	6	14
β-strand	98-101	4	14
β-strand	104	1	14
β-strand	110-117	8	14
β-strand	122-125	4	6
β-strand	135-140	6	15
α-helix	141-151	11
β-strand	157-161	5	11
β-strand	166-173	8	11
β-strand	176-183	8	11
β-strand	196-199	4	15
β-strand	204-208	5	11
α-helix	209-215	7
α-helix	216-221	6
β-strand	224-229	6	15
β-strand	235-241	7	15
β-strand	245-251	7	15
β-strand	254	1	5

Chain C: 8 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	13
α-helix	10-20	11
β-strand	26-29	4	16
β-strand	34-40	7	16
β-strand	46-53	8	16
α-helix	54-56	3
β-strand	59-62	4	13
β-strand	67-70	4	16
α-helix	72-80	9
β-strand	87-92	6	13
β-strand	98-104	7	13
β-strand	110-117	8	13
α-helix	118	1
β-strand	119	1	16
β-strand	122-124	3	10
β-strand	135-140	6	16
α-helix	141-151	11
β-strand	157-160	4	17
β-strand	161	1	14
β-strand	166-173	8	14
β-strand	176-183	8	14
α-helix	191-193	3
β-strand	196-199	4	16
β-strand	205-208	4	17
α-helix	209-215	7
α-helix	216-221	6
β-strand	224-229	6	16
β-strand	235-241	7	16
β-strand	245-251	7	16
β-strand	254	1	9

Chain X: 20 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	6-11	6
β-strand	20-21	2	1
α-helix	23-26	4
β-strand	31-34	4	1
α-helix	35-43	9
α-helix	62-76	15
β-strand	81-85	5	1
α-helix	89-90	2
α-helix	138-148	11
β-strand	152-154	3	1
α-helix	159-169	11
β-strand	174-176	3	1
α-helix	181-184	4
β-strand	189-192	4	1
α-helix	202-203	2
β-strand	204-208	5	1
α-helix	209-216	8
α-helix	220-231	12
α-helix	243-252	10
α-helix	256-260	5
α-helix	269-271	3
α-helix	276-284	9
α-helix	291-293	3
α-helix	303-308	6
α-helix	309-313	5
α-helix	318-332	15
β-strand	337	1	2
α-helix	340-343	4
β-strand	345-351	7	3

Chain Y: 18 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	6-13	8
α-helix	15-17	3
β-strand	18-21	4	4
α-helix	23-26	4
β-strand	30-34	5	4
α-helix	35-43	9
α-helix	62-76	15
β-strand	80-85	6	4
α-helix	95-100	6
α-helix	136-139	4
α-helix	141-144	4
β-strand	152-154	3	4
α-helix	159-167	9
β-strand	174-176	3	4
α-helix	181-184	4
β-strand	189-192	4	4
α-helix	202-203	2
β-strand	204-208	5	4
α-helix	209-215	7
α-helix	220-231	12
α-helix	243-252	10
α-helix	256-262	7
α-helix	278-282	5
α-helix	303-307	5
α-helix	318-331	14
β-strand	337	1	5
β-strand	348-351	4	6

Chain Z: 19 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	6-13	8
α-helix	15-17	3
β-strand	18-19	2	7
α-helix	23-26	4
β-strand	30-34	5	7
α-helix	35-43	9
α-helix	52-53	2
α-helix	62-75	14
β-strand	80-85	6	7
β-strand	96	1	8
β-strand	98	1	8
α-helix	105-108	4
α-helix	138-148	11
β-strand	152-154	3	7
α-helix	159-168	10
β-strand	174-176	3	7
α-helix	180-182	3
β-strand	189-192	4	7
β-strand	205-208	4	7
α-helix	209-216	8
α-helix	220-231	12
α-helix	244-246	3
α-helix	276-282	7
α-helix	304-308	5
α-helix	309-313	5
α-helix	318-329	12
α-helix	336	1
β-strand	337	1	9
α-helix	338	1
β-strand	349-351	3	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Flap endonuclease-1	X, Y, Z	protein	379	Homo sapiens	P39748 (AlphaFold model)
Proliferating cell nuclear antigen	A, B, C	protein	261	Homo sapiens	P12004 (AlphaFold model)

Sequence of entity 1 (X, Y, Z), FASTA

>1UL1_1 Flap endonuclease-1 (chains X, Y, Z)
GIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQFLIAVRQGGDVLQNEEGETT
SHLMGMFYRTIRMMENGIKPVYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQ
EVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASCAALVKAGKVYAAATEDMD
CLTFGSPVLMRHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGI
GPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLFLEPEVLDPESVELKWSEP
NEEELIKFMCGEKQFSEERIRSGVKRLSKSRQGSTQGRLDDFFKVTGSLSSAKRKEPEPK
GSTKKKAKTGAAGKFKRGK

Sequence of entity 2 (A, B, C), FASTA

>1UL1_2 Proliferating cell nuclear antigen (chains A, B, C)
MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTY
RCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMD
LDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNI
KLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYK
IADMGHLKYYLAPKIEDEEGS

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	4

Primary citation

Structural basis for recruitment of human flap endonuclease 1 to PCNA. Sakurai, S., Kitano, K., Yamaguchi, H. et al. EMBO J (2005) 24:683-693. DOI 10.1038/sj.emboj.7600519 · 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

About this viewer

MolViewer shows 1UL1 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.