4ABO: Tubulin beta chain

Mal3 CH domain homology model and mammalian tubulin (2XRP) docked into the 8.6-Angstrom cryo-EM map of Mal3-GTPgammaS-microtubules. Determined by electron microscopy at 8.6 Å resolution. Released 6 Jun 2012.

Method: Electron microscopy
Resolution: 8.6 Å
Organisms: SUS SCROFA, SCHIZOSACCHAROMYCES POMBE
Chains: 9
Atoms: 27,996
Mol. weight: 421.06 kDa
Ligands: GTP, GSP
Released: 6 Jun 2012

Explore 4ABO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ABO contains 171 α-helices and 123 β-strands across 9 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 and G: 21 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	4	1	1
β-strand	6-9	4	1
α-helix	12-26	15
β-strand	30	1	2
β-strand	36	1	2
α-helix	49-52	4
β-strand	55	1	3
β-strand	61	1	3
β-strand	65-69	5	1
α-helix	72-78	7
α-helix	83-85	3
α-helix	89-91	3
β-strand	92-94	3	1
α-helix	105-109	5
α-helix	111-126	16
β-strand	134-139	6	1
α-helix	144-148	5
α-helix	149-160	12
β-strand	165-170	6	1
α-helix	184-194	11
β-strand	200-202	3	1
α-helix	206-214	9
α-helix	224-242	19
β-strand	248	1	4
α-helix	252-259	8
β-strand	267-268	2	1
β-strand	269-271	3	4
α-helix	289-295	7
α-helix	307-309	3
β-strand	312-320	9	4
α-helix	325-338	14
β-strand	351-356	6	4
β-strand	375-381	7	4
α-helix	382-384	3
α-helix	385-399	15
α-helix	403-405	3
α-helix	406-409	4
α-helix	415-436	22

Chains B, D and H: 20 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	5
α-helix	10-26	17
β-strand	65-69	5	5
α-helix	73-78	6
β-strand	92-94	3	5
α-helix	103-107	5
α-helix	109-128	20
β-strand	134-139	6	5
α-helix	144-149	6
α-helix	150-160	11
β-strand	165	1	5
β-strand	167-170	4	5
α-helix	184-194	11
β-strand	200-203	4	5
α-helix	206-215	10
α-helix	224-242	19
α-helix	252-259	8
β-strand	269-271	3	5
β-strand	277	1	6
α-helix	284-287	4
α-helix	288-294	7
α-helix	298-300	3
β-strand	312-321	10	5
α-helix	325-336	12
β-strand	343	1	5
β-strand	351-355	5	5
β-strand	368	1	6
β-strand	373-381	9	5
α-helix	382-384	3
α-helix	385-399	15
α-helix	403-405	3
α-helix	406-409	4
α-helix	415-429	15
α-helix	431-434	4

Chain F: 20 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	17
α-helix	10-26	17
β-strand	65-69	5	17
α-helix	73-78	6
β-strand	92-94	3	17
α-helix	103-107	5
α-helix	109-128	20
β-strand	134-139	6	17
α-helix	144-149	6
α-helix	150-160	11
β-strand	165	1	17
β-strand	167-170	4	17
α-helix	184-194	11
β-strand	200-203	4	17
α-helix	206-215	10
α-helix	224-242	19
α-helix	252-259	8
β-strand	269-271	3	17
β-strand	277	1	18
α-helix	284-287	4
α-helix	288-294	7
α-helix	298-300	3
β-strand	312-321	10	17
α-helix	325-336	12
β-strand	351-355	5	17
β-strand	368	1	18
β-strand	373-381	9	17
α-helix	382-384	3
α-helix	385-399	15
α-helix	403-405	3
α-helix	406-409	4
α-helix	415-429	15
α-helix	431-434	4

Chain I: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	5-16	12
α-helix	23-28	6
α-helix	30-40	11
α-helix	55-72	18
α-helix	80-83	4
α-helix	88-105	18
α-helix	113-117	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tubulin beta chain	A, C, E, G	protein	445	SUS SCROFA	P02554 (AlphaFold model)
Tubulin alpha-1A chain	B, D, F, H	protein	451	SUS SCROFA	P02550 (AlphaFold model)
Microtubule integrity protein MAL3	I	protein	145	SCHIZOSACCHAROMYCES POMBE	Q10113 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>4ABO_1 TUBULIN BETA CHAIN (chains A, C, E, G)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATADEQGEFEEEGEEDEA

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

>4ABO_2 TUBULIN ALPHA-1A CHAIN (chains B, D, F, H)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRGHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYEPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Sequence of entity 3 (I), FASTA

>4ABO_3 MICROTUBULE INTEGRITY PROTEIN MAL3 (chains I)
GAMGSESRQELLAWINQVTSLGLTRIEDCGKGYAMIQIFDSIYQDIPLKKVNFECNNEYQ
YINNWKVLQQVFLKKGIDKVVDPERLSRCKMQDNLEFVQWAKRFWDQYYPGGDYDALARR
GNRGPANTRVMNSSAGATGPSRRRQ

Ligands and cofactors

ID	Name	Formula	Copies
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	4
GSP	5'-guanosine-diphosphate-monothiophosphate	C10 H16 N5 O13 P3 S	4

Primary citation

Ebs Recognize a Nucleotide-Dependent Structural CAP at Growing Microtubule Ends. Maurer, S.P., Fourniol, F.J., Bohner, G. et al. Cell (2012) 149:371. DOI 10.1016/J.CELL.2012.02.049 · PubMed

Other PDB entries of the same protein (UniProt P02554 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9U6A 1.92 Å, Tubulin-DARPin D1 in complex with a flavone
7TTF 2.1 Å, Tubulin-RB3_SLD in complex with compound 12k
7L05 2.21 Å, Complex of novel maytansinoid M24 bound to T2R-TTL (two tubulin alpha/beta heterodimers,…
5JQG 2.24 Å, An apo tubulin-RB-TTL complex structure used for side-by-side comparison
5XKH 2.25 Å, Crystal structure of T2R-TTL-CF1 complex
7TTD 2.27 Å, Tubulin-RB3_SLD in complex with compound 12e
5XP3 2.3 Å, Crystal structure of apo T2R-TTL
6XES 2.32 Å, Tubulin-RB3_SLD in complex with compound 40a
7EMJ 2.33 Å, Crystal structure of T2R-TTL-Barbigerone complex
7XQY 2.35 Å, Crystal structure of T2R-TTL-15 complex
7EXC 2.39 Å, Crystal structure of T2R-TTL-1129A2 complex
6LS4 2.4 Å, A novel anti-tumor agent S-40 in complex with tubulin

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