7UN1: Sperm acrosome-associated protein 9

8-nm repeat of the human sperm tip singlet microtubule. Determined by electron microscopy at 6.0 Å resolution. Released 5 Oct 2022.

Method: Electron microscopy
Resolution: 6.0 Å
Organism: Homo sapiens
Chains: 109
Atoms: 290,845
Mol. weight: 4672.06 kDa
Ligands: GDP, GTP, MG
Released: 5 Oct 2022

Explore 7UN1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7UN1 contains 1,983 α-helices and 1,362 β-strands across 109 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: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	2-20	19
α-helix	22-36	15
α-helix	42-43	2
α-helix	46-55	10
α-helix	60-84	25
α-helix	91-103	13
α-helix	121-124	4
α-helix	127-128	2
α-helix	129-133	5
α-helix	135-157	23

Chain AB: 26 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	12
α-helix	10-27	18
β-strand	30	1	13
β-strand	36	1	13
α-helix	41-45	5
α-helix	47-49	3
β-strand	51-54	4	14
β-strand	56	1	15
β-strand	58-61	4	14
β-strand	63-67	5	12
α-helix	71-77	7
α-helix	87-89	3
β-strand	91-92	2	12
α-helix	109-111	3
α-helix	113-125	13
β-strand	130-136	7	12
α-helix	142-158	17
β-strand	164-167	4	12
β-strand	169-170	2	16
α-helix	171-172	2
α-helix	181-194	14
β-strand	198-200	3	12
β-strand	202-203	2	16
α-helix	204-209	6
α-helix	210-214	5
α-helix	222-235	14
α-helix	238-241	4
β-strand	246	1	17
α-helix	250-257	8
α-helix	261-263	3
β-strand	265-266	2	12
β-strand	267-270	4	18
α-helix	276-279	4
α-helix	286-293	8
α-helix	296-298	3
β-strand	299	1	18
α-helix	305-307	3
β-strand	310-314	5	18
β-strand	315-318	4	17
α-helix	324-336	13
β-strand	341	1	18
β-strand	351-353	3	17
α-helix	356-358	3
β-strand	364-365	2	17
β-strand	366-371	6	18
α-helix	372-374	3
α-helix	375-390	16
α-helix	395-399	5
α-helix	406-426	21

Chain AC: 22 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	30
α-helix	11-27	17
β-strand	54-55	2	31
β-strand	61-62	2	31
β-strand	65-69	5	30
α-helix	72-78	7
α-helix	82-85	4
α-helix	89-91	3
β-strand	92-94	3	30
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-126	16
β-strand	132-138	7	30
α-helix	144	1
α-helix	145-149	5
α-helix	150-160	11
β-strand	166-172	7	30
α-helix	173-174	2
α-helix	183-191	9
β-strand	200-205	6	30
α-helix	206-215	10
α-helix	224-243	20
β-strand	248	1	32
α-helix	254-259	6
β-strand	271-273	3	32
α-helix	278-283	6
α-helix	288-293	6
β-strand	312-320	9	32
α-helix	325-337	13
β-strand	343	1	32
β-strand	351-356	6	32
α-helix	359-361	3
β-strand	374-381	8	32
α-helix	384-400	17
α-helix	405-409	5
α-helix	416-435	20

Chain AD: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	2-9	8	46
α-helix	10-20	11
α-helix	24-27	4
β-strand	30	1	47
β-strand	36	1	47
β-strand	51-54	4	48
β-strand	56	1	49
β-strand	58-61	4	48
β-strand	63-67	5	46
α-helix	71-77	7
α-helix	80-82	3
α-helix	87-89	3
β-strand	90-92	3	46
α-helix	101-102	2
α-helix	103-107	5
α-helix	109-111	3
α-helix	113-125	13
β-strand	129-136	8	46
α-helix	142-158	17
β-strand	163-170	8	46
α-helix	181-195	15
β-strand	198-203	6	46
α-helix	204-210	7
α-helix	211-215	5
α-helix	222-224	3
α-helix	225-235	11
β-strand	246	1	50
α-helix	250-257	8
β-strand	265-266	2	46
β-strand	269-270	2	50
α-helix	286-293	8
β-strand	299	1	50
α-helix	305-307	3
β-strand	310-318	9	50
α-helix	324-336	13
β-strand	341	1	50
β-strand	349-354	6	50
α-helix	356-358	3
β-strand	364-371	8	50
α-helix	374-390	17
α-helix	395-399	5
α-helix	406-424	19

Chain AE: 22 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	61
α-helix	11-27	17
β-strand	35	1	62
β-strand	53-55	3	63
β-strand	60	1	62
β-strand	61-63	3	63
β-strand	65-68	4	61
α-helix	72-78	7
α-helix	89-91	3
β-strand	92-93	2	61
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-113	3
α-helix	115-127	13
β-strand	132-138	7	61
α-helix	144-147	4
α-helix	151-160	10
β-strand	165-172	8	61
α-helix	173-174	2
α-helix	183-194	12
β-strand	200-205	6	61
α-helix	206-215	10
α-helix	224-243	20
β-strand	248	1	61
α-helix	252-258	7
β-strand	269-273	5	61
α-helix	278-283	6
α-helix	288-294	7
β-strand	301	1	61
β-strand	312-321	10	61
α-helix	325-337	13
β-strand	343	1	61
β-strand	351-356	6	61
α-helix	359-363	5
β-strand	373-381	9	61
α-helix	384-398	15
α-helix	399-401	3
α-helix	405-409	5
α-helix	417-435	19

Chain AF: 20 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	2-9	8	70
α-helix	10-28	19
β-strand	30	1	71
β-strand	36	1	71
β-strand	51-54	4	72
β-strand	58-61	4	72
β-strand	63-67	5	70
α-helix	70-77	8
α-helix	87-89	3
β-strand	90-92	3	70
α-helix	101-102	2
α-helix	103-107	5
α-helix	109-111	3
α-helix	113-125	13
β-strand	129-136	8	70
α-helix	142-155	14
β-strand	163-168	6	70
α-helix	181-194	14
β-strand	198-201	4	70
α-helix	204-214	11
α-helix	222-234	13
α-helix	238-241	4
β-strand	246	1	73
α-helix	250-256	7
β-strand	260	1	74
β-strand	263	1	74
β-strand	265-266	2	70
β-strand	269-270	2	73
α-helix	286-294	9
β-strand	299	1	73
α-helix	305-307	3
β-strand	310-318	9	73
α-helix	323-336	14
β-strand	350-354	5	73
α-helix	356-358	3
β-strand	364-371	8	73
α-helix	374-390	17
α-helix	396-399	4
α-helix	406-425	20

Chain B: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	2-20	19
α-helix	22-36	15
α-helix	46-56	11
α-helix	60-86	27
α-helix	91-103	13
α-helix	127-128	2
α-helix	129-133	5
α-helix	135-157	23

Chain BA: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	2-8	7	101
α-helix	10-26	17
β-strand	30	1	102
β-strand	36	1	102
α-helix	41-45	5
α-helix	47-49	3
β-strand	51-53	3	103
α-helix	55-57	3
β-strand	59-61	3	103
β-strand	63-64	2	101
β-strand	65-67	3	104
α-helix	70-77	8
α-helix	82-84	3
β-strand	90-92	3	104
α-helix	101-102	2
α-helix	103-107	5
α-helix	110-125	16
β-strand	129-136	8	101
α-helix	142-158	17
β-strand	163-170	8	101
α-helix	181-192	12
β-strand	198-203	6	101
α-helix	204-209	6
α-helix	210-214	5
α-helix	222-236	15
β-strand	246	1	105
α-helix	250-255	6
β-strand	265-266	2	101
β-strand	267-270	4	105
α-helix	276-279	4
α-helix	286-293	8
α-helix	305-307	3
β-strand	310-318	9	105
α-helix	324-336	13
β-strand	341	1	105
β-strand	349	1	105
β-strand	352-354	3	105
α-helix	357-358	2
β-strand	365-371	7	105
α-helix	374-390	17
α-helix	396-399	4
α-helix	405-424	20

101 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Sperm acrosome-associated protein 9	A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, d, e, f, g, h, i, j, k, l	protein	222	Homo sapiens	Q96E40 (AlphaFold model)
Tubulin beta-4B chain	AB, AD, AF, BA, BD, BF, CB, CD, CF, DB, DD, DF, EB, ED, EF, FD, FF, FH, GD, GF, GH, HD, HF, HH, ID, IF, IH, JD, JF, KD, KF, KH, LB, LD, LF, MB, MD, MF	protein	445	Homo sapiens	P68371 (AlphaFold model)
Tubulin alpha-1A chain	AC, AE, BC, BE, BG, CC, CE, CG, DC, DE, DG, EC, EE, EG, FC, FE, FG, GC, GE, GG, HC, HE, HG, IC, IE, IG, JC, JE, JG, KC, KE, KG, LA, LC, LE, MA, MC, ME	protein	451	Homo sapiens	Q71U36 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, d, e, f, g, h, i, j, k, l), FASTA

>7UN1_1 Sperm acrosome-associated protein 9 (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, d, e, f, g, h, i, j, k, l)
MNEVKESLRSIEQKYKLFQQQQLTFTAALEHCRENAHDKIRPISSIGQVQSYMEHYCNSS
TDRRVLLMFLDICSELNKLCQHFEAVHSGTPVTNNLLEKCKTLVSQSNDLSSLRAKYPHD
VVNHLSCDEARNHYGGVVSLIPLILDLMKEWIAHSEKLPRKVLQHVSEPQAHQESTRGAA
RPAQAIGTQPRATKHKCRQLTKASLKPRGCSKPPWRPPGGKL

Sequence of entity 2 (AB, AD, AF, BA, BD, BF, CB, CD, CF, DB, DD, DF, EB, ED, EF, FD, FF, FH, GD, GF, GH, HD, HF, HH, ID, IF, IH, JD, JF, KD, KF, KH, LB, LD, LF, MB, MD, MF), FASTA

>7UN1_2 Tubulin beta-4B chain (chains AB, AD, AF, BA, BD, BF, CB, CD, CF, DB, DD, DF, EB, ED, EF, FD, FF, FH, GD, GF, GH, HD, HF, HH, ID, IF, IH, JD, JF, KD, KF, KH, LB, LD, LF, MB, MD, MF)
MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVYYNEATGGKYV
PRAVLVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATAEEEGEFEEEAEEEVA

Sequence of entity 3 (AC, AE, BC, BE, BG, CC, CE, CG, DC, DE, DG, EC, EE, EG, FC, FE, FG, GC, GE, GG, HC, HE, HG, IC, IE, IG, JC, JE, JG, KC, KE, KG, LA, LC, LE, MA, MC, ME), FASTA

>7UN1_3 Tubulin alpha-1A chain (chains AC, AE, BC, BE, BG, CC, CE, CG, DC, DE, DG, EC, EE, EG, FC, FE, FG, GC, GE, GG, HC, HE, HG, IC, IE, IG, JC, JE, JG, KC, KE, KG, LA, LC, LE, MA, MC, ME)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	38
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	38
MG	Magnesium ion	Mg	38

Primary citation

SPACA9 is a lumenal protein of human ciliary singlet and doublet microtubules. Gui, M., Croft, J.T., Zabeo, D. et al. Proc Natl Acad Sci U S A (2022) 119:e2207605119-e2207605119. DOI 10.1073/pnas.2207605119 · PubMed

Other PDB entries of the same protein (UniProt Q96E40 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7UNG 3.6 Å, 48-nm repeat of the human respiratory doublet microtubule
8J07 4.1 Å, 96nm repeat of human respiratory doublet microtubule and associated axonemal complexes

Browse structure collections

About this viewer

MolViewer shows 7UN1 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.