6QVJ: PDB entry 6QVJ

HsCKK (human CAMSAP1) decorated 14pf taxol-GDP microtubule. Determined by electron microscopy at 3.8 Å resolution. Released 27 Nov 2019.

Method: Electron microscopy
Resolution: 3.8 Å
Organism: Homo sapiens
Chains: 5
Atoms: 14,643
Mol. weight: 223.16 kDa
Ligands: TA1, GDP, MG, GTP
Released: 27 Nov 2019

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

Secondary structure: helices and β-sheets

6QVJ contains 89 α-helices and 85 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, 6 β-strands

Element	Residues	Length	Sheet
α-helix	4-10	7
α-helix	11-15	5
α-helix	22-29	8
β-strand	39-44	6	1
β-strand	51-57	7	1
β-strand	65-66	2	1
β-strand	80-87	8	1
β-strand	92-95	4	1
β-strand	107-110	4	1
α-helix	112-114	3

Chain O: 22 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	2
α-helix	11-27	17
β-strand	54-55	2	3
β-strand	61-62	2	3
β-strand	65-66	2	2
β-strand	68	1	4
α-helix	75-77	3
α-helix	82-85	4
β-strand	93	1	4
α-helix	103-106	4
α-helix	115-126	12
β-strand	134-140	7	2
α-helix	144-160	17
β-strand	165-172	8	2
α-helix	173-174	2
α-helix	183-187	5
α-helix	189-192	4
β-strand	202-205	4	2
α-helix	207-214	8
α-helix	224-238	15
α-helix	240-243	4
β-strand	248	1	2
α-helix	252-259	8
β-strand	269-273	5	2
α-helix	279-281	3
α-helix	307-309	3
β-strand	312-314	3	5
β-strand	319-321	3	2
α-helix	325-335	11
β-strand	343	1	5
β-strand	355-356	2	2
α-helix	362-363	2
β-strand	373-379	7	2
β-strand	380-381	2	5
α-helix	385-388	4
α-helix	393-396	4
α-helix	405-408	4
α-helix	409-411	3
α-helix	416-436	21

Chain S: 23 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3-8	6	12
α-helix	10-28	19
β-strand	30	1	13
β-strand	35	1	14
β-strand	36	1	13
α-helix	42-47	4
α-helix	49-51	3
β-strand	53-56	4	14
β-strand	60-63	4	14
β-strand	65-69	5	12
α-helix	73-80	8
β-strand	92-94	3	12
α-helix	105-109	5
α-helix	111-113	3
α-helix	116-127	12
β-strand	132-138	7	12
β-strand	140	1	15
α-helix	145-148	4
α-helix	150-160	11
β-strand	165-168	4	12
α-helix	170	1
β-strand	171-172	2	15
α-helix	173-174	2
α-helix	183-191	9
β-strand	200-202	3	12
β-strand	204-205	2	15
α-helix	207-211	5
α-helix	212-216	5
α-helix	224-237	14
α-helix	238-240	3
β-strand	248	1	16
α-helix	254-257	4
β-strand	267-268	2	12
β-strand	269-273	5	16
α-helix	280-283	4
α-helix	288-295	8
β-strand	312-321	10	16
α-helix	326-337	12
β-strand	343	1	16
β-strand	351-355	5	16
β-strand	373-381	9	16
α-helix	387-400	14
α-helix	409-411	3
α-helix	415-437	23

Chain U: 21 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3-8	6	17
α-helix	10-27	18
β-strand	30	1	18
β-strand	36	1	18
α-helix	42-47	4
α-helix	49-51	3
β-strand	53-55	3	19
α-helix	57-59	3
β-strand	61-63	3	19
β-strand	65-67	3	17
β-strand	68-69	2	20
α-helix	73-80	8
β-strand	93-94	2	20
α-helix	105-109	5
α-helix	116-126	11
β-strand	132-138	7	17
β-strand	140	1	21
α-helix	145-148	4
α-helix	150-160	11
β-strand	165-168	4	17
β-strand	171-172	2	21
α-helix	183-191	9
β-strand	200-202	3	17
β-strand	204-205	2	21
α-helix	207-214	8
α-helix	224-226	3
α-helix	228-238	11
β-strand	248	1	22
α-helix	254-257	4
β-strand	267-268	2	17
β-strand	269-273	5	22
α-helix	280-283	4
α-helix	288-295	8
α-helix	298-300	3
β-strand	312-320	9	22
α-helix	325-337	13
β-strand	343	1	22
β-strand	351-355	5	22
β-strand	374-381	8	22
α-helix	387-400	14
α-helix	409-411	3
α-helix	417-437	21

Chain X: 19 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	6
β-strand	6-9	4	7
α-helix	10-24	15
α-helix	48-51	4
β-strand	53-55	3	8
β-strand	61-63	3	8
β-strand	65-68	4	7
α-helix	73-80	8
α-helix	82-85	4
β-strand	93	1	7
α-helix	115-123	9
β-strand	132	1	6
β-strand	134-140	7	7
α-helix	145-160	16
β-strand	165-172	8	7
α-helix	173-174	2
α-helix	183-194	12
β-strand	200-205	6	7
α-helix	207-214	8
α-helix	224-238	15
α-helix	240-243	4
β-strand	248	1	9
α-helix	252-258	7
β-strand	269-273	5	7
α-helix	307-309	3
β-strand	312	1	10
β-strand	314	1	11
β-strand	317-321	5	7
α-helix	325-335	11
β-strand	343	1	10
β-strand	353-354	2	7
β-strand	355	1	9
α-helix	361-363	3
β-strand	373-379	7	7
β-strand	380	1	11
α-helix	385-391	7
α-helix	393-400	8
α-helix	406-409	4
α-helix	416-436	21

Molecules and chains

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

Sequence of entity 1 (I), FASTA

>6QVJ_1 Calmodulin-regulated spectrin-associated protein 1 (chains I)
MGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRGSGPKLFKEPSSKSNKPIIHNAISHCCL
AGKVNEPHKNSILEELEKCDANHYIILFRDAGCQFRALYCYYPDTEEIYKLTGTGPKNIT
KKMIDKLYKYSSDRKQFNLIPAKTMSVSVDALTIHNHLWQPKRPAVPKKAQTRK

Sequence of entity 2 (O, X), FASTA

>6QVJ_2 Tubulin alpha-1B chain (chains O, X)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Sequence of entity 3 (S, U), FASTA

>6QVJ_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 Q5T5Y3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6QUS 3.7 Å, HsCKK (human CAMSAP1) decorated 13pf taxol-GDP microtubule
5M5C 4.8 Å, Mechanism of microtubule minus-end recognition and protection by CAMSAP proteins
5M54 8.0 Å, Mechanism of microtubule minus-end recognition and protection by CAMSAP proteins

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