1SA1: Tubulin alpha chain

Tubulin-podophyllotoxin: stathmin-like domain complex. Determined by X-ray diffraction at 4.2 Å resolution. Released 23 Mar 2004.

Method: X-ray diffraction
Resolution: 4.2 Å
Organisms: Bos taurus, Rattus norvegicus
Chains: 5
Atoms: 14,180
Mol. weight: 219.67 kDa
Ligands: POD, GDP, GTP, MG
Released: 23 Mar 2004

Explore 1SA1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1SA1 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: 20 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	1
α-helix	11-28	18
β-strand	65-69	5	1
α-helix	74-80	7
α-helix	89-91	3
β-strand	92-94	3	1
α-helix	103-104	2
α-helix	105-110	6
α-helix	111-126	16
β-strand	132-140	9	1
α-helix	144-160	17
β-strand	165-172	8	1
α-helix	183-195	13
β-strand	200-205	6	1
α-helix	206-215	10
α-helix	224-238	15
α-helix	241-244	4
α-helix	253-257	5
β-strand	269	1	2
β-strand	277	1	3
α-helix	290-293	4
α-helix	298-300	3
α-helix	311	1
β-strand	312-318	7	2
β-strand	320-321	2	4
α-helix	325-337	13
β-strand	343	1	2
β-strand	352-355	4	2
β-strand	368	1	3
β-strand	373-374	2	4
β-strand	378-381	4	2
α-helix	382-384	3
α-helix	385-399	15
α-helix	406-411	6
α-helix	415-435	21

Chain B: 22 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	5
α-helix	11-28	18
β-strand	30	1	6
β-strand	36	1	6
α-helix	44-49	4
α-helix	50-52	3
β-strand	53	1	7
β-strand	63	1	7
β-strand	65-68	4	5
α-helix	76-79	4
α-helix	89-91	3
β-strand	92-93	2	5
α-helix	103-107	5
α-helix	109-112	4
α-helix	115-126	12
β-strand	134-140	7	5
α-helix	149-157	9
β-strand	165-172	8	5
α-helix	183-197	15
β-strand	200-205	6	5
α-helix	206-214	9
α-helix	225-243	19
β-strand	267-268	2	5
β-strand	269-272	4	8
α-helix	289-295	7
α-helix	298-300	3
β-strand	301	1	8
β-strand	312-321	10	8
α-helix	325-333	9
α-helix	335-338	4
β-strand	351-354	4	8
β-strand	373-381	9	8
α-helix	382-384	3
α-helix	385-398	14
α-helix	404-407	4
α-helix	409-411	3
α-helix	415-432	18
α-helix	433-435	3

Chain C: 17 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	9
α-helix	11-28	18
β-strand	65-69	5	9
α-helix	74-78	5
β-strand	92-94	3	9
α-helix	103-104	2
α-helix	105-110	6
α-helix	111-126	16
β-strand	132-140	9	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	224-238	15
β-strand	269	1	10
β-strand	277	1	11
α-helix	290-293	4
α-helix	298-300	3
α-helix	311	1
β-strand	312	1	12
β-strand	316-317	2	13
β-strand	320-321	2	14
α-helix	325-337	13
β-strand	343	1	12
β-strand	352-353	2	13
β-strand	368	1	11
β-strand	373-374	2	14
β-strand	379	1	10
β-strand	381	1	12
α-helix	382-384	3
α-helix	385-399	15
α-helix	406-411	6
α-helix	415-435	21

Chain D: 19 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	15
α-helix	11-28	18
β-strand	30	1	16
β-strand	36	1	16
α-helix	44-52	7
β-strand	65-68	4	15
α-helix	76-79	4
α-helix	89-91	3
β-strand	92-93	2	15
α-helix	103-107	5
α-helix	109-126	18
β-strand	134-140	7	15
α-helix	149-157	9
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	267	1
β-strand	268	1	15
β-strand	269-272	4	17
α-helix	289-295	7
α-helix	298-300	3
β-strand	301	1	17
β-strand	312-321	10	17
α-helix	325-335	11
β-strand	351-354	4	17
β-strand	373-381	9	17
α-helix	382-384	3
α-helix	385-398	14
α-helix	406-409	4
α-helix	415-432	18
α-helix	433-435	3

Chain E: 8 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	13-14	2	2
β-strand	17-19	3	2
α-helix	55-66	12
α-helix	70-82	13
α-helix	84-97	14
α-helix	99-103	5
α-helix	106-112	7
α-helix	114-117	4
α-helix	119-125	7
α-helix	127-130	4

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

>1SA1_1 Tubulin alpha chain (chains A, C)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYEPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Sequence of entity 2 (B, D), FASTA

>1SA1_2 Tubulin beta chain (chains B, D)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATADEQGEFEEEGEEDEA

Sequence of entity 3 (E), FASTA

>1SA1_3 Stathmin 4 (chains E)
ADMEVIELNKCTSGQSFEVILKPPSFDGVPEFNASLPRRRDPSLEEIQKKLEAAEERRKY
QEAELLKHLAEKREHEREVIQKAIEENNNFIKMAKEKLAQKMESNKENREAHLAAMLERL
QEKDKHAEEVRKNKELKEEASR

Ligands and cofactors

ID	Name	Formula	Copies
POD	9-hydroxy-5-(3,4,5-trimethoxyphenyl)-5,8,8A,9-TETRAHYDROFURO[3',4':6,7]NAPHTHO[…	C22 H22 O8	2
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	2
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	2
MG	Magnesium ion	Mg	2

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)
1SA0 3.58 Å, Tubulin-colchicine: stathmin-like domain complex
1Z2B 4.1 Å, Tubulin-colchicine-vinblastine: 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…

Browse structure collections

About this viewer

MolViewer shows 1SA1 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.