6I2I: Refined 13pf Hela Cell Tubulin microtubule

Refined 13pf Hela Cell Tubulin microtubule (EML4-NTD decorated). Determined by electron microscopy at 3.6 Å resolution. Released 28 Aug 2019.

Method: Electron microscopy
Resolution: 3.6 Å
Organism: Homo sapiens
Chains: 2
Atoms: 6,830
Mol. weight: 101.87 kDa
Ligands: G2P, TA1, MG, GTP
Released: 28 Aug 2019

Explore 6I2I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6I2I contains 45 α-helices and 34 β-strands across 2 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: 24 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	1
α-helix	11-28	18
β-strand	53-55	3	2
β-strand	61-63	3	2
β-strand	65-68	4	1
α-helix	73-80	8
α-helix	82-84	3
β-strand	93	1	1
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-126	16
β-strand	132-140	9	1
α-helix	145-148	4
α-helix	150-160	11
β-strand	165-172	8	1
α-helix	183-189	7
α-helix	190-193	4
β-strand	200-201	2	1
β-strand	204-205	2	1
α-helix	207-210	4
α-helix	212-215	4
α-helix	224-227	4
α-helix	229-238	10
α-helix	240-243	4
α-helix	254-259	6
β-strand	268-270	3	3
β-strand	273	1	4
α-helix	288-291	4
α-helix	293-296	4
β-strand	312-314	3	3
β-strand	317-318	2	5
β-strand	319-321	3	4
α-helix	325-337	13
β-strand	343	1	3
β-strand	353-354	2	5
α-helix	359-360	2
β-strand	373-375	3	4
β-strand	378-381	4	3
α-helix	384-387	4
α-helix	389-396	8
α-helix	405-407	3
α-helix	416-436	21

Chain B: 21 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	6
α-helix	13-28	16
β-strand	30	1	7
β-strand	36	1	7
α-helix	41-44	4
α-helix	49-51	3
β-strand	53-56	4	8
β-strand	60-63	4	8
β-strand	65-68	4	6
α-helix	72-80	9
β-strand	93	1	6
α-helix	105-109	5
α-helix	111-113	3
α-helix	115-125	11
β-strand	132-139	8	6
α-helix	144-147	4
α-helix	152-160	9
β-strand	165-172	8	6
α-helix	185-195	11
β-strand	200-205	6	6
α-helix	208-211	4
α-helix	212-216	5
α-helix	224-238	15
α-helix	252-258	7
β-strand	267-268	2	6
α-helix	288-295	8
α-helix	307-309	3
β-strand	312-320	9	9
α-helix	325-338	14
α-helix	340-342	3
β-strand	343	1	9
β-strand	353-356	4	9
β-strand	374	1	9
β-strand	377-381	5	9
α-helix	385-400	16
α-helix	406-409	4
α-helix	416-432	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tubulin alpha-1B chain	A	protein	451	Homo sapiens	P68363 (AlphaFold model)
Tubulin beta chain	B	protein	444	Homo sapiens	P07437 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6I2I_1 Tubulin alpha-1B chain (chains A)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Sequence of entity 2 (B), FASTA

>6I2I_2 Tubulin beta chain (chains B)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQVFDAKNMM
AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATAEEEEDFGEEAEEEA

Ligands and cofactors

ID	Name	Formula	Copies
G2P	Phosphomethylphosphonic acid guanylate ester	C11 H18 N5 O13 P3	1
TA1	Taxol	C47 H51 N O14	1
MG	Magnesium ion	Mg	2
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	1

Primary citation

Mitotic phosphorylation by NEK6 and NEK7 reduces the microtubule affinity of EML4 to promote chromosome congression. Adib, R., Montgomery, J.M., Atherton, J. et al. Sci Signal (2019) 12. DOI 10.1126/scisignal.aaw2939 · 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

Browse structure collections

About this viewer

MolViewer shows 6I2I 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.