6TX2: Human HPF1

Human HPF1. Determined by X-ray diffraction at 2.09 Å resolution. Released 19 Feb 2020.

Method: X-ray diffraction
Resolution: 2.09 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,679
Mol. weight: 36.78 kDa
Released: 19 Feb 2020

Explore 6TX2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6TX2 contains 15 α-helices and 7 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: 15 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	38-45	8
α-helix	51-63	13
α-helix	68-70	3
α-helix	73-76	4
β-strand	79-80	2	1
α-helix	83-87	5
β-strand	115-120	6	1
β-strand	127-132	6	1
β-strand	142-147	6	1
β-strand	155-156	2	1
α-helix	161-173	13
α-helix	179-199	21
α-helix	208-214	7
β-strand	219	1	2
β-strand	227	1	2
α-helix	245-256	12
α-helix	261-267	7
α-helix	269-283	15
α-helix	288-300	13
α-helix	303-305	3
α-helix	306-319	14
α-helix	323-334	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone PARylation factor 1	A	protein	318	Homo sapiens	Q9NWY4 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6TX2_1 Histone PARylation factor 1 (chains A)
MGHHHHHHLRKEVENHYKLSLPEDFYHFWKFCEELDPEKPSDSLSASLGLQLVGPYDILA
GKHKTKKKSTGLNFNLHWRFYYDPPEFQTIIIGDNKTQYHMGYFRDSPDEFPVYVGINEA
KKNCIIVPNGDNVFAAVKLFLTKKLKEITDKKKINLLKNIDEKLTEAARELGYSLEQRTV
KMKQRDKKVVTKTFHGAGLVVPVDKNDVGYRELPETDADLKRICKTIVEAASDEERLKAF
APIQEMMTFVQFANDECDYGMGLELGMDLFCYGSHYFHKVAGQLLPLAYNLLKRNLFAEI
IEEHLANRSQENIDQLAA

Primary citation

HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation. Suskiewicz, M.J., Zobel, F., Ogden, T.E.H. et al. Nature (2020) 579:598-602. DOI 10.1038/s41586-020-2013-6 · PubMed

Other PDB entries of the same protein (UniProt Q9NWY4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6M3G 1.57 Å, Crystal structure of human HPF1
6M3I 1.98 Å, Crystal structure of HPF1/PARP1 complex
6TX3 2.96 Å, HPF1 bound to catalytic fragment of PARP2
6X0L 3.9 Å, Bridging of double-strand DNA break activates PARP2/HPF1 to modify chromatin
9MJA 4.3 Å, PARP1 ART in complex with HPF1 and EB47
6X0M 6.3 Å, Bridging of double-strand DNA break activates PARP2/HPF1 to modify chromatin
6X0N 10.0 Å, Bridging of double-strand DNA break activates PARP2/HPF1 to modify chromatin

Browse structure collections

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