1SA0: Tubulin-colchicine: stathmin-like domain complex

Tubulin-colchicine: stathmin-like domain complex. Determined by X-ray diffraction at 3.58 Å resolution. Released 23 Mar 2004.

Method: X-ray diffraction
Resolution: 3.58 Å
Organisms: Bos taurus, Rattus norvegicus
Chains: 5
Atoms: 14,074
Mol. weight: 219.72 kDa
Ligands: GDP, CN2, GTP, MG
Released: 23 Mar 2004

Explore 1SA0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1SA0 contains 86 α-helices and 64 β-strands across 5 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: 23 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	1
α-helix	10-28	19
β-strand	53	1	2
β-strand	63	1	2
β-strand	65-69	5	1
α-helix	74-78	5
α-helix	89-91	3
β-strand	92-94	3	1
α-helix	103-104	2
α-helix	105-109	5
α-helix	110-125	16
β-strand	134-140	7	1
α-helix	144-160	17
β-strand	165-172	8	1
α-helix	183-193	11
α-helix	194-197	4
β-strand	200-205	6	1
α-helix	206-215	10
α-helix	224-240	17
α-helix	241-245	5
α-helix	252-259	8
α-helix	268	1
β-strand	269-270	2	3
β-strand	277	1	4
α-helix	285-287	3
α-helix	288-293	6
α-helix	298-300	3
β-strand	312	1	5
β-strand	316-321	6	6
α-helix	325-337	13
β-strand	343	1	5
β-strand	352-356	5	6
β-strand	368	1	4
α-helix	369-370	2
β-strand	373-374	2	6
β-strand	378-379	2	3
β-strand	381	1	5
α-helix	383-385	3
α-helix	386-399	14
α-helix	406-411	6
α-helix	415-434	20

Chain B: 20 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	7
α-helix	11-28	18
α-helix	42-44	3
α-helix	49-52	4
β-strand	65-68	4	7
α-helix	73-79	7
α-helix	84-86	3
α-helix	89-91	3
β-strand	92-93	2	7
α-helix	103-107	5
α-helix	109-126	18
β-strand	134-140	7	7
α-helix	150-157	8
β-strand	165-172	8	7
α-helix	183-197	15
β-strand	200-205	6	7
α-helix	206-214	9
α-helix	225-243	19
α-helix	254-259	6
β-strand	267-268	2	7
β-strand	269-272	4	8
α-helix	289-295	7
α-helix	298-300	3
β-strand	301	1	8
β-strand	312-320	9	8
α-helix	325-338	14
β-strand	343	1	8
β-strand	351-356	6	8
β-strand	374-381	8	8
α-helix	382-384	3
α-helix	385-395	11
α-helix	406-409	4
α-helix	416-432	17

Chain C: 20 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	9
α-helix	10-28	19
α-helix	49-51	3
β-strand	53	1	10
β-strand	63	1	10
β-strand	65-69	5	9
α-helix	74-78	5
β-strand	92-94	3	9
α-helix	103-104	2
α-helix	105-109	5
α-helix	110-125	16
β-strand	134-140	7	9
α-helix	144-160	17
β-strand	165-172	8	9
α-helix	183-195	13
β-strand	200-205	6	9
α-helix	206-215	10
α-helix	224-240	17
α-helix	256-258	3
α-helix	268	1
β-strand	269-270	2	11
β-strand	277	1	12
α-helix	288-293	6
α-helix	298-300	3
β-strand	312	1	13
β-strand	316-321	6	14
α-helix	325-337	13
β-strand	343	1	13
β-strand	352-356	5	14
β-strand	368	1	12
α-helix	369-370	2
β-strand	373-374	2	14
β-strand	378-379	2	11
β-strand	381	1	13
α-helix	383-385	3
α-helix	386-399	14
α-helix	406-411	6
α-helix	415-434	20

Chain D: 18 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	15
α-helix	11-28	18
α-helix	42-52	9
β-strand	65-68	4	15
α-helix	73-79	7
α-helix	89-91	3
β-strand	92-93	2	15
α-helix	103-107	5
α-helix	109-128	20
β-strand	134-140	7	15
α-helix	150-157	8
β-strand	165-172	8	15
α-helix	183-197	15
β-strand	200-205	6	15
α-helix	206-214	9
α-helix	225-243	19
α-helix	254-259	6
β-strand	267-268	2	15
β-strand	269-272	4	16
α-helix	289-295	7
α-helix	298-300	3
β-strand	301	1	16
β-strand	312-320	9	16
α-helix	325-338	14
β-strand	343	1	16
β-strand	351-356	6	16
β-strand	374-381	8	16
α-helix	382-384	3
α-helix	385-395	11
α-helix	406-409	4
α-helix	416-432	17

Chain E: 5 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	9	1	6
β-strand	18-21	4	6
α-helix	54-56	3
α-helix	58-70	13
α-helix	73-97	25
α-helix	107-121	15
α-helix	131-133	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tubulin alpha chain	A, C	protein	451	Bos taurus	Q2HJ86 (AlphaFold model)
Tubulin beta chain	B, D	protein	445	Bos taurus	Q6B856 (AlphaFold model)
Stathmin 4	E	protein	142	Rattus norvegicus	P63043 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1SA0_1 Tubulin alpha chain (chains A, C)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYEPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Sequence of entity 2 (B, D), FASTA

>1SA0_2 Tubulin beta chain (chains B, D)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATADEQGEFEEEGEEDEA

Sequence of entity 3 (E), FASTA

>1SA0_3 Stathmin 4 (chains E)
ADMEVIELNKCTSGQSFEVILKPPSFDGVPEFNASLPRRRDPSLEEIQKKLEAAEERRKY
QEAELLKHLAEKREHEREVIQKAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERL
QEKDKHAEEVRKNKELKEEASR

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	2
CN2	2-mercapto-N-[1,2,3,10-tetramethoxy-9-oxo-5,6,7,9-tetrahydro-benzo[a]heptalen-7…	C22 H25 N O6 S	2
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	2
MG	Magnesium ion	Mg	3

Primary citation

Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Ravelli, R.B., Gigant, B., Curmi, P.A. et al. Nature (2004) 428:198-202. DOI 10.1038/nature02393 · PubMed

Other PDB entries of the same protein (UniProt Q2HJ86 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1TVK 2.89 Å, The binding mode of epothilone A on a,b-tubulin by electron crystallography
7RRO 3.4 Å, Structure of the 48-nm repeat doublet microtubule from bovine tracheal cilia
9CPB 3.52 Å, Atomic model of bovine Fallopian tube cilia doublet microtubule (48-nm periodicity)
1Z2B 4.1 Å, Tubulin-colchicine-vinblastine: stathmin-like domain complex
1SA1 4.2 Å, Tubulin-podophyllotoxin: stathmin-like domain complex
2XRP 8.2 Å, Human Doublecortin N-DC Repeat (1MJD) and Mammalian Tubulin (1JFF and 3HKE) Docked into…
4ATX 8.2 Å, Rigor kinesin motor domain with an ordered neck-linker, docked on tubulin dimer,…
4ATU 8.3 Å, Human doublecortin N-DC repeat plus linker, and tubulin (2XRP) docked into an 8A cryo-EM…
3IZ0 8.6 Å, Human Ndc80 Bonsai Decorated Microtubule
4CK6 9.2 Å, Pseudo-atomic model of microtubule-bound human kinesin-5 motor domain in the ADP.AlFx…
4CK7 9.2 Å, Pseudo-atomic model of microtubule-bound human kinesin-5 motor domain in presence of…
5M5I 9.3 Å, Pseudo-atomic model of microtubule-bound S.pombe kinesin-5 motor domain in the AMPPNP…

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