8R2O: Huntingtin-Q17, 1-66, N-MBP fusion

Huntingtin-Q17, 1-66, N-MBP fusion. Determined by X-ray diffraction at 3.23 Å resolution. Released 18 Sept 2024.

Method: X-ray diffraction
Resolution: 3.23 Å
Organism: Homo sapiens
Chains: 2
Atoms: 6,514
Mol. weight: 97.83 kDa
Released: 18 Sept 2024

Explore 8R2O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8R2O contains 46 α-helices and 50 β-strands across 2 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: 24 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	4	1	1
β-strand	6-10	5	1
α-helix	17-31	15
β-strand	34-38	5	1
α-helix	43-50	8
β-strand	59-63	5	1
α-helix	65-72	8
β-strand	76-77	2	1
α-helix	78	1
β-strand	79	1	2
α-helix	83-88	6
β-strand	89	1	3
α-helix	91-96	6
β-strand	98-99	2	2
β-strand	102-103	2	2
β-strand	105-111	7	1
β-strand	114-118	5	4
α-helix	125-126	2
β-strand	128	1	5
α-helix	131-141	11
β-strand	145	1	6
α-helix	154-163	10
β-strand	167-172	6	7
β-strand	175-182	8	7
α-helix	186-200	15
α-helix	210-218	9
β-strand	222	1	6
β-strand	224-227	4	4
α-helix	229-231	3
α-helix	233-237	5
β-strand	242-245	4	4
α-helix	246-248	3
β-strand	249	1	5
β-strand	250	1	8
β-strand	253	1	8
β-strand	258-259	2	9
β-strand	260-267	8	1
α-helix	273-279	7
α-helix	280-284	5
α-helix	287-296	10
β-strand	301-302	2	1
β-strand	304	1	3
α-helix	305-311	7
α-helix	315-326	12
β-strand	328-329	2	9
α-helix	330-331	2
α-helix	336-351	16
α-helix	357-370	14
α-helix	373-375	3
α-helix	376-408	33

Chain B: 22 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	6-10	5	10
α-helix	17-31	15
β-strand	34-38	5	10
α-helix	43-50	8
β-strand	59-62	4	10
α-helix	65-72	8
β-strand	76	1	11
α-helix	77-79	3
α-helix	83-86	4
β-strand	89	1	12
α-helix	91-96	6
β-strand	98	1	13
β-strand	103	1	13
β-strand	105-110	6	10
β-strand	114-118	5	14
β-strand	128	1	15
α-helix	132-141	10
β-strand	145	1	16
α-helix	154-162	9
β-strand	169-171	3	17
β-strand	176-181	6	17
α-helix	186-200	15
α-helix	210-218	9
β-strand	222	1	16
β-strand	224-227	4	14
α-helix	229-232	4
α-helix	233-237	5
β-strand	242-245	4	14
α-helix	246-248	3
β-strand	249-250	2	15
β-strand	253-254	2	15
β-strand	258-259	2	18
β-strand	261-266	6	10
β-strand	267	1	11
α-helix	273-279	7
α-helix	280-284	5
α-helix	287-296	10
β-strand	301-302	2	10
β-strand	304	1	12
α-helix	305-311	7
α-helix	315-326	12
β-strand	328-329	2	18
α-helix	330-331	2
α-helix	336-351	16
α-helix	357-370	14
α-helix	376-408	33

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Maltodextrin-binding protein,Huntingtin, myristoylated N-terminal fragment	A, B	protein	442	Homo sapiens	A0ACD6BAW2

Sequence of entity 1 (A, B), FASTA

>8R2O_1 Maltodextrin-binding protein,Huntingtin, myristoylated N-terminal fragment (chains A, B)
MGMKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP
DIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIY
NKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYD
IKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDT
SKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDK
PLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTV
DAALAAAQTNAAAGSENLYFQGMATLEKLMKAFESLKSFQQQQQQQQQQQQQQQQQPPPP
PPPPPPPQLPQPPPQAQPLLPQ

Primary citation

Post-translational modifications of huntingtin's N17 region: implications for self-association and membrane binding. Gallo, M., Ingenito, R., Finotto, M. et al. Biochim Biophys Acta Mol Basis Dis (2025) 1871:168019-168019. DOI 10.1016/j.bbadis.2025.168019 · PubMed

Other PDB entries of the same protein (UniProt A0ACD6BAW2), best resolution first:

7KD5 1.55 Å, Structure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329…
6ZIS 1.73 Å, Crystal structure of a CGRP receptor ectodomain heterodimer with bound high affinity…
8ZLW 2.2 Å, Crystal Structure of RDGC IQ motif/dCaM Complex
5GXT 2.25 Å, Crystal structure of PigG
8R3E 2.91 Å, Huntingtin, 1-17, MBP-N
28QM 3.4 Å, MBP bound to distal DARPin (AHIR dodecamer scaffold system)

Browse structure collections

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