7SJ9: Tubulin alpha-1B chain

13pf E254A microtubule from recombinant human tubulin decorated with EB3. Determined by electron microscopy at 3.8 Å resolution. Released 19 Jan 2022.

Method: Electron microscopy
Resolution: 3.8 Å
Organism: Homo sapiens
Chains: 14
Atoms: 43,240
Mol. weight: 684.12 kDa
Ligands: MG, GTP
Released: 19 Jan 2022

Explore 7SJ9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7SJ9 contains 298 α-helices and 205 β-strands across 14 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.

Chains A and C: 24 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	1
α-helix	10-27	18
α-helix	48-50	3
β-strand	53-55	3	2
β-strand	61-63	3	2
β-strand	65-69	5	1
α-helix	72-80	9
α-helix	89-91	3
β-strand	92-94	3	1
α-helix	103-104	2
α-helix	105-109	5
α-helix	112-127	16
β-strand	134-140	7	1
α-helix	144	1
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-172	8	1
α-helix	173-174	2
α-helix	183-194	12
β-strand	200-205	6	1
α-helix	206-212	7
α-helix	213-217	5
α-helix	224-243	20
β-strand	248	1	1
α-helix	252-258	7
β-strand	262	1	3
β-strand	265	1	3
β-strand	269-273	5	1
α-helix	288-296	9
α-helix	307-309	3
β-strand	312-321	10	1
α-helix	325-337	13
β-strand	343	1	1
β-strand	351-356	6	1
α-helix	359-363	5
β-strand	373-381	9	1
α-helix	384-400	17
α-helix	405-409	5
α-helix	415-436	22
α-helix	438-440	3

Chain B: 22 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	4
α-helix	10-28	19
β-strand	30	1	5
β-strand	36	1	5
α-helix	42-45	4
α-helix	47-49	3
β-strand	51-54	4	6
β-strand	58-61	4	6
β-strand	63-67	5	4
α-helix	70-78	9
α-helix	87-89	3
β-strand	90-92	3	4
α-helix	101-102	2
α-helix	103-107	5
α-helix	110-126	17
β-strand	130-138	9	4
α-helix	142-158	17
β-strand	163-170	8	4
α-helix	171-172	2
α-helix	181-195	15
β-strand	198-200	3	4
β-strand	202-203	2	4
α-helix	204-213	10
α-helix	222-241	20
β-strand	246	1	7
α-helix	250-257	8
β-strand	265-266	2	4
β-strand	267-271	5	7
α-helix	286-293	8
α-helix	296-298	3
α-helix	305-307	3
β-strand	310-318	9	7
α-helix	323-336	14
β-strand	341	1	7
β-strand	349-353	5	7
β-strand	364-371	8	7
α-helix	372-374	3
α-helix	375-389	15
α-helix	395-399	5
α-helix	405-426	22

Chain D: 22 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	11
α-helix	10-28	19
β-strand	30	1	12
β-strand	36	1	12
α-helix	42-45	4
α-helix	47-49	3
β-strand	51-54	4	13
β-strand	58-61	4	13
β-strand	63-67	5	11
α-helix	70-78	9
α-helix	87-89	3
β-strand	90-92	3	11
α-helix	101-102	2
α-helix	103-107	5
α-helix	110-126	17
β-strand	130-138	9	11
α-helix	142-158	17
β-strand	163-170	8	11
α-helix	171-172	2
α-helix	181-195	15
β-strand	198-200	3	11
β-strand	202-203	2	11
α-helix	204-213	10
α-helix	222-241	20
β-strand	246	1	14
α-helix	250-257	8
β-strand	265-266	2	11
β-strand	267-271	5	14
α-helix	286-293	8
α-helix	296-298	3
β-strand	299	1	14
α-helix	305-307	3
β-strand	310-318	9	14
α-helix	323-335	13
β-strand	341	1	14
β-strand	349-353	5	14
β-strand	364-371	8	14
α-helix	372-374	3
α-helix	375-389	15
α-helix	395-399	5
α-helix	405-427	23

Chain E: 24 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	15
α-helix	10-27	18
β-strand	53-55	3	16
β-strand	61-63	3	16
β-strand	65-69	5	15
α-helix	72-80	9
α-helix	89-91	3
β-strand	92-94	3	15
α-helix	103-104	2
α-helix	105-109	5
α-helix	112-127	16
β-strand	134-140	7	15
α-helix	144	1
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-172	8	15
α-helix	173-174	2
α-helix	183-194	12
β-strand	200-205	6	15
α-helix	206-212	7
α-helix	213-217	5
α-helix	224-243	20
β-strand	248	1	15
α-helix	252-258	7
β-strand	262	1	17
β-strand	265	1	17
β-strand	269-273	5	15
α-helix	288-296	9
α-helix	298-300	3
α-helix	307-309	3
β-strand	312-321	10	15
α-helix	325-337	13
β-strand	343	1	15
β-strand	351-356	6	15
α-helix	359-363	5
β-strand	373-381	9	15
α-helix	384-400	17
α-helix	405-409	5
α-helix	415-436	22
α-helix	438-440	3

Chain F: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	18
α-helix	10-28	19
β-strand	30	1	19
β-strand	36	1	19
α-helix	42-45	4
α-helix	47-49	3
β-strand	51-54	4	20
β-strand	58-61	4	20
β-strand	63-67	5	18
α-helix	70-78	9
α-helix	87-89	3
β-strand	90-92	3	18
α-helix	101-102	2
α-helix	103-107	5
α-helix	110-126	17
β-strand	130-138	9	18
α-helix	142-158	17
β-strand	163-170	8	18
α-helix	171-172	2
α-helix	181-195	15
β-strand	198-200	3	18
β-strand	202-203	2	18
α-helix	204-213	10
α-helix	222-241	20
β-strand	246	1	21
α-helix	250-257	8
β-strand	265-266	2	18
β-strand	267-271	5	21
α-helix	286-293	8
α-helix	296-298	3
β-strand	299	1	21
α-helix	305-307	3
β-strand	310-318	9	21
α-helix	323-335	13
β-strand	341	1	21
β-strand	349-353	5	21
α-helix	356-358	3
β-strand	364-371	8	21
α-helix	372-374	3
α-helix	375-389	15
α-helix	395-399	5
α-helix	405-427	23

Chain G: 25 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	22
α-helix	10-28	19
β-strand	30	1	23
β-strand	36	1	23
α-helix	42-45	4
α-helix	47-49	3
β-strand	51-54	4	24
β-strand	58-61	4	24
β-strand	63-67	5	22
α-helix	70-78	9
α-helix	87-89	3
β-strand	90-92	3	22
α-helix	101-102	2
α-helix	103-107	5
α-helix	110-126	17
β-strand	130-138	9	22
α-helix	142	1
α-helix	143-147	5
α-helix	148-158	11
β-strand	163-170	8	22
α-helix	171-172	2
α-helix	181-195	15
β-strand	198-200	3	22
β-strand	202-203	2	22
α-helix	204-213	10
α-helix	222-241	20
β-strand	246	1	25
α-helix	250-257	8
β-strand	265-266	2	22
β-strand	267-271	5	25
α-helix	286-293	8
α-helix	296-298	3
α-helix	305-307	3
β-strand	310-318	9	25
α-helix	323-335	13
β-strand	341	1	25
β-strand	349-353	5	25
α-helix	356-358	3
β-strand	364-371	8	25
α-helix	372-374	3
α-helix	375-389	15
α-helix	395-399	5
α-helix	405-426	22

Chain H: 22 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	26
α-helix	10-28	19
β-strand	30	1	27
β-strand	36	1	27
α-helix	41-43	3
α-helix	47-49	3
β-strand	51-54	4	28
β-strand	58-61	4	28
β-strand	63-67	5	26
α-helix	70-78	9
α-helix	87-89	3
β-strand	90-92	3	26
α-helix	101-102	2
α-helix	103-107	5
α-helix	109-111	3
α-helix	113-126	14
β-strand	130-138	9	26
α-helix	142-158	17
β-strand	163-170	8	26
α-helix	171-172	2
α-helix	181-195	15
β-strand	198-200	3	26
β-strand	202-203	2	26
α-helix	204-213	10
α-helix	222-241	20
β-strand	246	1	29
α-helix	250-257	8
β-strand	265-266	2	26
β-strand	267-271	5	29
α-helix	286-293	8
α-helix	296-298	3
α-helix	305-307	3
β-strand	310-318	9	29
α-helix	323-335	13
β-strand	341	1	29
β-strand	349-353	5	29
β-strand	364-371	8	29
α-helix	374-389	16
α-helix	395-399	5
α-helix	405-426	22

Chain I: 22 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	30
α-helix	10-28	19
β-strand	30	1	31
β-strand	36	1	31
α-helix	42-45	4
α-helix	47-49	3
β-strand	51-53	3	32
β-strand	59-61	3	32
β-strand	63-67	5	30
α-helix	70-78	9
α-helix	87-89	3
β-strand	90-92	3	30
α-helix	101-102	2
α-helix	103-107	5
α-helix	109-111	3
α-helix	113-126	14
β-strand	130-138	9	30
α-helix	142-158	17
β-strand	163-170	8	30
α-helix	171-172	2
α-helix	181-195	15
β-strand	198-200	3	30
β-strand	202-203	2	30
α-helix	204-213	10
α-helix	222-241	20
β-strand	246	1	33
α-helix	250-257	8
β-strand	265-266	2	30
β-strand	267-271	5	33
α-helix	286-293	8
α-helix	296-298	3
α-helix	305-307	3
β-strand	310-318	9	33
α-helix	323-335	13
β-strand	341	1	33
β-strand	349-353	5	33
β-strand	359	1	34
β-strand	361	1	34
β-strand	364-371	8	33
α-helix	374-389	16
α-helix	395-399	5
α-helix	405-426	22

4 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
Tubulin alpha-1B chain	A, C, E, J, K, L	protein	457	Homo sapiens	P68363 (AlphaFold model)
Tubulin beta-3 chain	B, D, F, G, H, I	protein	456	Homo sapiens	Q13509 (AlphaFold model)
Microtubule-associated protein RP/EB family member 3	M, N	protein	281	Homo sapiens	Q9UPY8 (AlphaFold model)

Sequence of entity 1 (A, C, E, J, K, L), FASTA

>7SJ9_1 Tubulin alpha-1B chain (chains A, C, E, J, K, L)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIHHHHHHGGGDDSFNTFFS
ETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEI
IDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPA
PQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQI
VSSITASLRFDGALNVDLTAFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNA
CFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVG
INYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGME
EGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Sequence of entity 2 (B, D, F, G, H, I), FASTA

>7SJ9_2 Tubulin beta-3 chain (chains B, D, F, G, H, I)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVYYNEASSHKYV
PRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTARGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVATVFRGRMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRG
LKMSSTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATAEEEGEMYEDDEEESEAQGPKENLYFQ

Sequence of entity 3 (M, N), FASTA

>7SJ9_3 Microtubule-associated protein RP/EB family member 3 (chains M, N)
MAVNVYSTSVTSENLSRHDMLAWVNDSLHLNYTKIEQLCSGAAYCQFMDMLFPGCVHLRK
VKFQAKLEHEYIHNFKVLQAAFKKMGVDKIIPVEKLVKGKFQDNFEFIQWFKKFFDANYD
GKDYNPLLARQGQDVAPPPNPGDQIFNKSKKLIGTAVPQRTSPTGPKNMQTSGRLSNVAP
PCILRKNPPSARNGGHETDAQILELNQQLVDLKLTVDGLEKERDFYFSKLRDIELICQEH
ESENSPVISGIIGILYATEEGFAPPEDDEIEEHQQEDQDEY

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	12
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	12

Primary citation

Structural transitions in the GTP cap visualized by cryo-electron microscopy of catalytically inactive microtubules. LaFrance, B.J., Roostalu, J., Henkin, G. et al. Proc Natl Acad Sci U S A (2022) 119. DOI 10.1073/pnas.2114994119 · PubMed

Other PDB entries of the same protein (UniProt P68363 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6S8L 1.8 Å, Structure, Thermodynamics, and Kinetics of Plinabulin Binding to two Tubulin Isotypes
6J8O 1.85 Å, Structure of a hypothetical protease
7PJF 1.86 Å, Inhibiting parasite proliferation using a rationally designed anti-tubulin agent
6J4V 2.1 Å, Structural basis of tubulin detyrosination by vasohibins-SVBP enzyme complex and…
8VT7 2.66 Å, Structure of the gamma tubulin ring complex nucleated microtubule protofilament.
7Z6S 2.9 Å, MATCAP bound to a human 14 protofilament microtubule
8V2J 2.9 Å, Structure of alpha1B and betaI/IVb microtubule bound to GDP
9COC 2.9 Å, Two protofilament structure of alpha1B and betaI/IVb microtubule bound to GDP
9BP6 3.1 Å, Structure of alpha1B and betaI/IVb microtubule bound to GMPCPP
9CMM 3.1 Å, Two protofilament structure of alpha1B and betaI/IVb microtubule bound to GMPCPP
7LXB 3.26 Å, HeLa-tubulin in complex with cryptophycin 52
9HQ4 3.28 Å, TTLL11 bound to microtubule

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