6QUS: Tubulin alpha-1B chain

HsCKK (human CAMSAP1) decorated 13pf taxol-GDP microtubule. Determined by electron microscopy at 3.7 Å resolution. Released 27 Nov 2019.

Method: Electron microscopy
Resolution: 3.7 Å
Organism: Homo sapiens
Chains: 5
Atoms: 14,715
Mol. weight: 223.16 kDa
Ligands: TA1, GDP, MG, GTP
Released: 27 Nov 2019

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

Secondary structure: helices and β-sheets

6QUS contains 87 α-helices and 80 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 I: 4 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	1487-1493	7
α-helix	1494-1498	5
α-helix	1505-1515	11
β-strand	1522-1527	6	9
β-strand	1534-1540	7	9
β-strand	1541	1	10
β-strand	1546	1	10
β-strand	1549-1552	4	9
β-strand	1565-1570	6	9
β-strand	1575-1579	5	9
β-strand	1590-1592	3	9
α-helix	1595-1597	3

Chain O: 22 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	6
α-helix	10-27	18
β-strand	53-54	2	7
β-strand	62-63	2	7
β-strand	65-66	2	6
β-strand	68	1	8
α-helix	73-78	6
β-strand	93	1	8
α-helix	103-106	4
α-helix	115-126	12
β-strand	134-138	5	6
α-helix	144	1
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-172	8	6
α-helix	173-174	2
α-helix	183-194	12
β-strand	200-205	6	6
α-helix	207-215	9
α-helix	224-238	15
β-strand	248	1	6
α-helix	252-258	7
β-strand	269-273	5	6
α-helix	288-291	4
α-helix	307-309	3
β-strand	312-316	5	6
β-strand	318-321	4	6
α-helix	325-333	9
β-strand	343	1	6
β-strand	354-355	2	6
α-helix	359-363	5
α-helix	369-370	2
β-strand	373-381	9	6
α-helix	382-384	3
α-helix	385-391	7
α-helix	393-400	8
α-helix	406-409	4
α-helix	417-436	20

Chain S: 20 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	16
α-helix	10-24	15
β-strand	30	1	17
β-strand	35	1	18
β-strand	36	1	17
α-helix	42-47	4
α-helix	49-51	3
β-strand	53-55	3	19
α-helix	56	1
β-strand	60	1	18
β-strand	61-63	3	19
β-strand	65-68	4	16
α-helix	73-80	8
β-strand	93	1	16
α-helix	105-109	5
α-helix	116-127	12
β-strand	132-138	7	16
α-helix	145-158	14
β-strand	165-171	7	16
α-helix	172-174	3
α-helix	183-194	12
β-strand	200-204	5	16
α-helix	207-211	5
α-helix	212-216	5
α-helix	224-239	16
α-helix	254-257	4
β-strand	267-268	2	16
β-strand	269-273	5	20
α-helix	280-282	3
α-helix	288-295	8
β-strand	301	1	20
β-strand	312-321	10	20
α-helix	325-337	13
β-strand	343	1	20
β-strand	351-355	5	20
β-strand	373-381	9	20
α-helix	385-400	16
α-helix	406-409	4
α-helix	415-436	22

Chain U: 21 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	11
α-helix	10-25	16
β-strand	30	1	12
β-strand	36	1	12
α-helix	41-43	3
α-helix	49-51	3
β-strand	53-55	3	13
β-strand	61-63	3	13
β-strand	65-69	5	11
α-helix	73-80	8
β-strand	93-94	2	11
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-113	3
α-helix	115-127	13
β-strand	132-138	7	11
β-strand	140	1	14
α-helix	145-160	16
β-strand	165-168	4	11
β-strand	171	1	14
α-helix	172-174	3
α-helix	183-197	15
β-strand	200-202	3	11
β-strand	204	1	14
α-helix	207-211	5
α-helix	212-216	5
α-helix	224-238	15
β-strand	246-248	3	15
α-helix	254-257	4
β-strand	267-268	2	11
β-strand	269-273	5	15
α-helix	280-282	3
α-helix	288-295	8
β-strand	312-319	8	15
α-helix	325-337	13
β-strand	343	1	15
β-strand	351-356	6	15
β-strand	375-381	7	15
α-helix	385-400	16
α-helix	406-409	4
α-helix	416-437	22

Chain X: 20 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	65-68	4	1
α-helix	75-78	4
α-helix	103-106	4
α-helix	115-126	12
β-strand	134-140	7	1
α-helix	144	1
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-171	7	1
β-strand	172	1	3
α-helix	173-174	2
α-helix	183-197	15
β-strand	200-202	3	1
β-strand	203	1	4
β-strand	205	1	3
α-helix	207-214	8
α-helix	224-238	15
β-strand	248	1	5
α-helix	252-258	7
β-strand	269-273	5	4
β-strand	312-321	10	4
α-helix	325-333	9
α-helix	335-337	3
β-strand	343	1	4
β-strand	353-354	2	4
β-strand	355	1	5
α-helix	359-363	5
α-helix	369-370	2
β-strand	373-381	9	4
α-helix	384-399	16
α-helix	406-409	4
α-helix	417-436	20

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tubulin alpha-1B chain	O, X	protein	451	Homo sapiens	P68363 (AlphaFold model)
Calmodulin-regulated spectrin-associated protein 1	I	protein	174	Homo sapiens	Q5T5Y3 (AlphaFold model)
Tubulin beta chain	S, U	protein	444	Homo sapiens	P07437 (AlphaFold model)

Sequence of entity 1 (O, X), FASTA

>6QUS_1 Tubulin alpha-1B chain (chains O, X)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Sequence of entity 2 (I), FASTA

>6QUS_2 Calmodulin-regulated spectrin-associated protein 1 (chains I)
MGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRGSGPKLFKEPSSKSNKPIIHNAISHCCL
AGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYYPDTEEIYKLTGTGPKNIT
KKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKRPAVPKKAQTRK

Sequence of entity 3 (S, U), FASTA

>6QUS_3 Tubulin beta chain (chains S, U)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQVFDAKNMM
AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATAEEEEDFGEEAEEEA

Ligands and cofactors

ID	Name	Formula	Copies
TA1	Taxol	C47 H51 N O14	2
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	2
MG	Magnesium ion	Mg	2
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	2

Primary citation

Structural determinants of microtubule minus end preference in CAMSAP CKK domains. Atherton, J., Luo, Y., Xiang, S. et al. Nat Commun (2019) 10:5236-5236. DOI 10.1038/s41467-019-13247-6 · 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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