7KQ0: PCNA

PCNA bound to peptide mimetic. Determined by X-ray diffraction at 2.4 Å resolution. Released 19 May 2021.

Method: X-ray diffraction
Resolution: 2.4 Å
Organisms: Homo sapiens, synthetic construct
Chains: 6
Atoms: 6,086
Mol. weight: 91.84 kDa
Released: 19 May 2021

Explore 7KQ0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7KQ0 contains 30 α-helices and 66 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: 9 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	1
α-helix	10-19	10
β-strand	25-31	7	2
β-strand	34-40	7	2
β-strand	46-53	8	2
α-helix	54-56	3
β-strand	59-62	4	1
β-strand	66-71	6	2
α-helix	72-80	9
β-strand	87-92	6	1
β-strand	98-104	7	1
β-strand	111-117	7	1
β-strand	119	1	2
β-strand	126	1	3
β-strand	135-140	6	2
α-helix	141-151	11
β-strand	157-162	6	4
β-strand	166-173	8	4
β-strand	176-183	8	4
α-helix	184-185	2
α-helix	191-193	3
β-strand	196-199	4	2
β-strand	203-208	6	4
α-helix	209-215	7
α-helix	216-221	6
β-strand	224-230	7	2
β-strand	233-241	9	2
β-strand	245-251	7	2
α-helix	252-253	2
β-strand	254-255	2	4

Chain B: 1 helix, 2 β-strands

Element	Residues	Length	Sheet
β-strand	143-144	2	4
α-helix	147-149	3
β-strand	153	1	3

Chain C: 9 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	5
α-helix	9-19	11
β-strand	25-31	7	6
β-strand	34-40	7	6
β-strand	46-53	8	6
α-helix	54-56	3
β-strand	59-62	4	5
β-strand	66-71	6	6
α-helix	72-80	9
β-strand	87-92	6	5
β-strand	98-104	7	5
β-strand	111-117	7	5
α-helix	118	1
β-strand	119	1	6
β-strand	127	1	7
β-strand	135-140	6	6
α-helix	141-151	11
β-strand	157-162	6	8
β-strand	167-173	7	8
β-strand	176-182	7	8
α-helix	191-193	3
β-strand	196-199	4	6
β-strand	203-208	6	8
α-helix	209-215	7
α-helix	216-221	6
β-strand	224-229	6	6
β-strand	235-240	6	6
β-strand	246-251	6	6
α-helix	252-253	2
β-strand	254-255	2	8

Chain D: 1 helix, 2 β-strands

Element	Residues	Length	Sheet
β-strand	143-144	2	8
α-helix	147-149	3
β-strand	152	1	7

Chain E: 9 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	9
α-helix	9-19	11
β-strand	25-31	7	10
β-strand	34-40	7	10
β-strand	46-53	8	10
α-helix	54-56	3
β-strand	59-62	4	9
β-strand	66-71	6	10
α-helix	72-80	9
β-strand	87-92	6	9
β-strand	98-104	7	9
β-strand	111-117	7	9
β-strand	135-140	6	10
α-helix	141-151	11
β-strand	157-162	6	11
β-strand	166-173	8	11
β-strand	176-183	8	11
α-helix	184-185	2
α-helix	191-193	3
β-strand	196-199	4	10
β-strand	203-208	6	11
α-helix	209-215	7
α-helix	216-221	6
β-strand	224-229	6	10
β-strand	235-241	7	10
β-strand	245-251	7	10
α-helix	252-253	2
β-strand	254	1	11

Chain F: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
β-strand	144	1	11
α-helix	147-149	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Proliferating cell nuclear antigen	A, C, E	protein	259	Homo sapiens	P12004 (AlphaFold model)
Lys-arg-arg-gln-thr-ser-met-thr-asp-tyr-tyr-his-ser-lys-arg	B, D, F	protein	15	synthetic construct	P38936 (AlphaFold model)

Sequence of entity 1 (A, C, E), FASTA

>7KQ0_1 Proliferating cell nuclear antigen (chains A, C, E)
MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTY
RCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMD
LDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNI
KLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYK
IADMGHLKYYLAPKIEDEE

Sequence of entity 2 (B, D, F), FASTA

>7KQ0_2 LYS-ARG-ARG-GLN-THR-SER-MET-THR-ASP-TYR-TYR-HIS-SER-LYS-ARG (chains B, D, F)
KRRQTSMTDYYHSKR

Primary citation

Unlocking the PIP-box: A peptide library reveals interactions that drive high-affinity binding to human PCNA. Horsfall, A.J., Vandborg, B.A., Kowalczyk, W. et al. J Biol Chem (2021) 296:100773-100773. DOI 10.1016/j.jbc.2021.100773 · PubMed

Other PDB entries of the same protein (UniProt P12004 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1U7B 1.88 Å, Crystal structure of hPCNA bound to residues 331-350 of the flap endonuclease-1 (FEN1)
8F5Q 1.9 Å, Crystal structure of human PCNA in complex with the PIP box of FBH1
9N3L 1.9 Å, Co-crystal structure of PCNA bound to HSP90alpha inhibitor, SNX2112
5E0U 1.93 Å, Human PCNA variant (S228I) complexed with p21 at 1.9 Angstroms
5MLO 1.96 Å, Crystal structure of human PCNA in complex with ZRANB3 PIP box peptide
4RJF 2.01 Å, Crystal structure of the human sliding clamp at 2.0 angstrom resolution
5E0V 2.07 Å, Human PCNA variant (S228I) complexed with FEN1 at 2.1 Angstroms
3VKX 2.1 Å, Structure of PCNA
6HVO 2.1 Å, Crystal structure of human PCNA in complex with three peptides of p12 subunit of human…
4ZTD 2.2 Å, Crystal Structure of Human PCNA in complex with a TRAIP peptide
5YCO 2.2 Å, Complex structure of PCNA with UHRF2
5MOM 2.27 Å, Crystal Structure of PCNA encoding the hypomorphic mutation S228I

Browse structure collections

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