8R3E: Huntingtin, 1-17, MBP-N

Huntingtin, 1-17, MBP-N. Determined by X-ray diffraction at 2.91 Å resolution. Released 18 Sept 2024.

Method: X-ray diffraction
Resolution: 2.91 Å
Organism: Homo sapiens
Chains: 6
Atoms: 18,255
Mol. weight: 262.23 kDa
Ligands: ZN
Released: 18 Sept 2024

Explore 8R3E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8R3E contains 138 α-helices and 156 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: 22 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	7-10	4	1
α-helix	17-31	15
β-strand	35-38	4	1
α-helix	43-52	10
β-strand	59-63	5	1
α-helix	64-73	10
β-strand	76	1	2
α-helix	77-78	2
α-helix	83-88	6
β-strand	89	1	3
α-helix	91-94	4
β-strand	98-99	2	4
β-strand	102-103	2	4
β-strand	105-110	6	1
β-strand	112	1	5
β-strand	115-118	4	6
β-strand	128	1	7
α-helix	132-140	9
β-strand	145-147	3	6
α-helix	154-164	11
β-strand	167	1	8
β-strand	170-171	2	9
β-strand	176-177	2	9
β-strand	182	1	8
α-helix	186-200	15
α-helix	210-218	9
β-strand	222-226	5	6
α-helix	229-231	3
β-strand	242-245	4	6
α-helix	246-248	3
β-strand	249	1	7
β-strand	250	1	10
β-strand	253	1	10
α-helix	254-255	2
β-strand	258-259	2	5
β-strand	262-266	5	1
β-strand	267	1	2
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	315-325	11
β-strand	328-329	2	5
α-helix	330-331	2
α-helix	336-352	17
α-helix	357-368	12
α-helix	372-392	21

Chain B: 22 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	7-10	4	11
α-helix	17-31	15
β-strand	35-38	4	11
α-helix	43-52	10
β-strand	59-63	5	11
α-helix	64-73	10
β-strand	76-77	2	11
α-helix	78-79	2
α-helix	83-88	6
β-strand	89	1	12
α-helix	91-94	4
β-strand	98-99	2	13
β-strand	102-103	2	13
β-strand	105-110	6	11
β-strand	115-118	4	14
β-strand	128	1	15
α-helix	132-140	9
β-strand	145	1	16
α-helix	154-162	9
β-strand	167	1	17
β-strand	170-171	2	18
β-strand	176-177	2	18
β-strand	182	1	17
α-helix	186-200	15
α-helix	210-218	9
β-strand	222	1	16
β-strand	224-226	3	14
α-helix	229-234	6
β-strand	242-245	4	14
α-helix	246-248	3
β-strand	249	1	15
β-strand	250	1	19
β-strand	253	1	19
α-helix	254-255	2
β-strand	258-259	2	20
β-strand	262-267	6	11
α-helix	273-279	7
α-helix	280-284	5
α-helix	287-296	10
β-strand	301-302	2	11
β-strand	304	1	12
α-helix	305-311	7
α-helix	315-326	12
β-strand	328-329	2	20
α-helix	330-331	2
α-helix	336-352	17
α-helix	357-369	13
α-helix	371-393	23

Chain C: 23 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	7-10	4	21
α-helix	17-31	15
β-strand	35-38	4	21
α-helix	43-52	10
β-strand	59-63	5	21
α-helix	64-73	10
β-strand	76-77	2	21
α-helix	78	1
α-helix	83-88	6
β-strand	89	1	22
α-helix	91-94	4
β-strand	98-99	2	23
β-strand	102-103	2	23
β-strand	105-110	6	21
β-strand	114-118	5	24
β-strand	128	1	25
α-helix	132-140	9
β-strand	145-147	3	24
α-helix	154-163	10
β-strand	167	1	26
β-strand	170-172	3	27
β-strand	175-177	3	27
β-strand	182	1	26
α-helix	186-200	15
α-helix	210-218	9
β-strand	222-227	6	24
α-helix	229-231	3
α-helix	232-238	7
β-strand	242-245	4	24
α-helix	246-248	3
β-strand	249	1	25
β-strand	250	1	28
β-strand	253	1	28
α-helix	254-255	2
β-strand	258-259	2	29
β-strand	262-267	6	21
α-helix	273-279	7
α-helix	280-284	5
α-helix	287-296	10
β-strand	301-302	2	21
β-strand	304	1	22
α-helix	305-311	7
α-helix	315-326	12
β-strand	328-329	2	29
α-helix	330-331	2
α-helix	336-352	17
α-helix	357-368	12
α-helix	375-395	21

Chain D: 23 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	7-10	4	30
α-helix	17-31	15
β-strand	35-38	4	30
α-helix	43-52	10
β-strand	59-63	5	30
α-helix	64-73	10
β-strand	76-77	2	30
α-helix	78	1
α-helix	83-88	6
β-strand	89	1	31
α-helix	91-94	4
β-strand	98-99	2	32
β-strand	102-103	2	32
β-strand	105-110	6	30
β-strand	115-118	4	33
β-strand	128	1	34
α-helix	132-140	9
β-strand	145	1	35
α-helix	154-165	12
β-strand	167	1	36
β-strand	170-171	2	37
β-strand	176-177	2	37
β-strand	182	1	36
α-helix	186-200	15
α-helix	210-218	9
β-strand	222	1	35
β-strand	224-226	3	33
α-helix	229-231	3
α-helix	232-235	4
β-strand	242-245	4	33
α-helix	246-248	3
β-strand	249	1	34
β-strand	250	1	38
β-strand	253	1	38
α-helix	254-255	2
β-strand	258-259	2	39
β-strand	262-267	6	30
α-helix	273-279	7
α-helix	280-284	5
α-helix	287-296	10
β-strand	301-302	2	30
β-strand	304	1	31
α-helix	305-311	7
α-helix	315-326	12
β-strand	328-329	2	39
α-helix	330-331	2
α-helix	336-352	17
α-helix	357-368	12
α-helix	372-392	21

Chain E: 24 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	7-10	4	40
α-helix	17-31	15
β-strand	35-38	4	40
α-helix	43-52	10
β-strand	59-63	5	40
α-helix	64-73	10
β-strand	76	1	41
α-helix	77-78	2
α-helix	83-88	6
β-strand	89	1	42
α-helix	91-94	4
β-strand	98-99	2	43
β-strand	102-103	2	43
β-strand	105-107	3	40
β-strand	109-110	2	44
β-strand	112	1	45
β-strand	115-118	4	46
α-helix	129-131	3
α-helix	132-140	9
β-strand	145	1	47
α-helix	154-162	9
β-strand	167	1	48
β-strand	170-171	2	49
β-strand	176-177	2	49
β-strand	182	1	48
α-helix	186-200	15
α-helix	210-218	9
β-strand	222	1	47
β-strand	224-226	3	46
α-helix	229-231	3
α-helix	232-235	4
β-strand	242-245	4	46
α-helix	246-249	4
β-strand	250	1	50
β-strand	253	1	50
α-helix	254-255	2
β-strand	258-259	2	45
β-strand	262-266	5	40
β-strand	267	1	41
α-helix	273-279	7
α-helix	280-284	5
α-helix	287-296	10
β-strand	300-302	3	44
β-strand	304	1	42
α-helix	305-311	7
α-helix	315-326	12
β-strand	328-329	2	45
α-helix	330-331	2
α-helix	336-352	17
α-helix	357-369	13
α-helix	371-390	20

Chain F: 24 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	7-10	4	51
α-helix	17-31	15
β-strand	35-38	4	51
α-helix	43-52	10
β-strand	59-63	5	51
α-helix	64-73	10
β-strand	76-77	2	51
α-helix	78	1
α-helix	83-88	6
β-strand	89	1	52
α-helix	91-96	6
β-strand	98-99	2	53
β-strand	102-103	2	53
β-strand	105-110	6	51
β-strand	114-118	5	54
α-helix	125-126	2
β-strand	128	1	55
α-helix	132-139	8
α-helix	140-142	3
β-strand	145-147	3	54
α-helix	154-164	11
β-strand	167	1	56
β-strand	170-172	3	57
β-strand	175-177	3	57
β-strand	182	1	56
α-helix	186-200	15
α-helix	210-218	9
β-strand	222-227	6	54
α-helix	229-231	3
α-helix	232-235	4
β-strand	242-245	4	54
α-helix	246-248	3
β-strand	249	1	55
β-strand	250	1	58
β-strand	253	1	58
α-helix	254-255	2
β-strand	258-259	2	59
β-strand	262-267	6	51
α-helix	273-279	7
α-helix	280-284	5
α-helix	287-296	10
β-strand	301-302	2	51
β-strand	304	1	52
α-helix	305-311	7
α-helix	315-326	12
β-strand	328-329	2	59
α-helix	336-352	17
α-helix	357-368	12
α-helix	375-393	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Maltodextrin-binding protein	A, B, C, D, E, F	protein	399	Homo sapiens	A0ACD6BAW2

Sequence of entity 1 (A, B, C, D, E, F), FASTA

>8R3E_1 Maltodextrin-binding protein (chains A, B, C, D, E, F)
MGMKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP
DIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIY
NKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYD
IKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDT
SKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDK
PLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTV
DAALAAAQTNAAAGSENLYFQGMATLEKLMKAFESLKSF

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1

Primary citation

Post-translational modifications in the first 17 amino acids of huntingtin influence self-association and interaction with membranes. Gallo, M., Ingenito, R., Finotto, M. et al. To be published.

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
8R2O 3.23 Å, Huntingtin-Q17, 1-66, N-MBP fusion
28QM 3.4 Å, MBP bound to distal DARPin (AHIR dodecamer scaffold system)

Browse structure collections

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