7SJ8: Tubulin alpha-1B chain

13pf wildtype microtubule from recombinant human tubulin decorated with kinesin. Determined by electron microscopy at 3.6 Å resolution. Released 19 Jan 2022.

Method: Electron microscopy
Resolution: 3.6 Å
Organism: Homo sapiens
Chains: 12
Atoms: 41,056
Mol. weight: 619.8 kDa
Ligands: GTP, GDP, MG
Released: 19 Jan 2022

Explore 7SJ8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7SJ8 contains 295 α-helices and 216 β-strands across 12 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, C, E, J and K: 24 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	1
α-helix	10-27	18
α-helix	49-51	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	111-113	3
α-helix	115-128	14
β-strand	134-138	5	1
α-helix	144-160	17
β-strand	165-169	5	1
α-helix	172-174	3
α-helix	183-194	12
β-strand	200	1	1
β-strand	203	1	3
α-helix	206-215	10
α-helix	224-243	20
β-strand	248	1	3
α-helix	252-259	8
α-helix	268	1
β-strand	269-273	5	3
β-strand	277	1	4
α-helix	288-296	9
α-helix	298-300	3
β-strand	301	1	3
α-helix	307-309	3
β-strand	314-321	8	3
α-helix	325-337	13
β-strand	352-356	5	3
α-helix	359-363	5
β-strand	368	1	4
β-strand	373-380	8	3
α-helix	384-400	17
α-helix	405-410	6
α-helix	415-436	22
α-helix	438-440	3

Chains B, D, F, G, H and I: 25 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	3-8	6	50
α-helix	10-28	19
β-strand	30	1	51
β-strand	36	1	51
α-helix	41-45	5
α-helix	47-49	3
β-strand	51-54	4	52
β-strand	58-61	4	52
β-strand	63-65	3	50
β-strand	66-67	2	53
α-helix	70-78	9
α-helix	87-89	3
β-strand	91-92	2	53
α-helix	101-102	2
α-helix	103-107	5
α-helix	109-126	18
β-strand	130-138	9	50
α-helix	142	1
α-helix	143-147	5
α-helix	148-158	11
β-strand	163-170	8	50
α-helix	171-172	2
α-helix	181-195	15
β-strand	198-200	3	50
β-strand	202-203	2	50
α-helix	204-209	6
α-helix	210-214	5
α-helix	222-241	20
β-strand	246	1	54
α-helix	250-257	8
β-strand	265-266	2	50
β-strand	267-271	5	54
α-helix	286-292	7
α-helix	296-298	3
α-helix	305-307	3
β-strand	310-317	8	54
α-helix	323-336	14
α-helix	338-340	3
β-strand	341	1	54
β-strand	349-353	5	54
β-strand	365-371	7	54
α-helix	375-390	16
α-helix	395-399	5
α-helix	405-426	22

Chain L: 25 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	21
α-helix	10-27	18
α-helix	49-51	3
β-strand	53-55	3	22
β-strand	61-63	3	22
β-strand	65-69	5	21
α-helix	72-80	9
α-helix	89-91	3
β-strand	92-94	3	21
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-113	3
α-helix	115-128	14
β-strand	134-138	5	21
α-helix	144-160	17
β-strand	165-169	5	21
α-helix	172-174	3
α-helix	183-194	12
β-strand	200	1	21
β-strand	203	1	23
α-helix	206-215	10
α-helix	224-243	20
β-strand	248	1	23
α-helix	252-259	8
α-helix	268	1
β-strand	269-273	5	23
β-strand	277	1	24
α-helix	288-296	9
α-helix	298-300	3
β-strand	301	1	23
α-helix	307-309	3
β-strand	314-321	8	23
α-helix	325-337	13
β-strand	352-356	5	23
α-helix	359-360	2
α-helix	362-363	2
β-strand	368	1	24
β-strand	373-380	8	23
α-helix	384-400	17
α-helix	405-410	6
α-helix	415-436	22
α-helix	438-440	3

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)

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

>7SJ8_1 Tubulin alpha-1B chain (chains A, C, E, J, K, L)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIHHHHHHGGGDDSFNTFFS
ETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEI
IDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPA
PQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQI
VSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNA
CFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVG
INYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGME
EGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY

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

>7SJ8_2 Tubulin beta-3 chain (chains B, D, F, G, H, I)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVYYNEASSHKYV
PRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTARGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVATVFRGRMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRG
LKMSSTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATAEEEGEMYEDDEEESEAQGPKENLYFQ

Ligands and cofactors

ID	Name	Formula	Copies
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	6
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	6
MG	Magnesium ion	Mg	6

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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