9EDR: Chromosome instability protein 1

Tubulin Cofactors D,E,G,C and Tubulin complex -- TBCC N Terminus Bound to Tubulin. Determined by electron microscopy at 3.8 Å resolution. Released 4 Feb 2026.

Method: Electron microscopy
Resolution: 3.8 Å
Organisms: Saccharomyces cerevisiae, Sus scrofa, Escherichia coli
Chains: 7
Atoms: 21,378
Mol. weight: 329.64 kDa
Ligands: GDP, GTP
Released: 4 Feb 2026

Explore 9EDR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9EDR contains 165 α-helices and 95 β-strands across 7 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: 26 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-9	7	6
α-helix	10-28	19
β-strand	35	1	7
α-helix	49-51	3
β-strand	53-55	3	8
β-strand	60	1	7
β-strand	61-63	3	8
β-strand	65-69	5	6
α-helix	72-80	9
α-helix	89-91	3
β-strand	92-94	3	6
α-helix	103-104	2
α-helix	105-109	5
α-helix	110-127	18
β-strand	132-140	9	6
α-helix	144-160	17
β-strand	165-172	8	6
α-helix	175-177	3
α-helix	183-195	13
β-strand	200-205	6	6
α-helix	206-212	7
α-helix	213-217	5
α-helix	224-243	20
α-helix	252-259	8
α-helix	268	1
β-strand	269-273	5	9
β-strand	277	1	10
α-helix	280-282	3
α-helix	288-294	7
α-helix	298-300	3
β-strand	301	1	9
α-helix	307-309	3
β-strand	312-321	10	9
α-helix	325-338	14
α-helix	342	1
β-strand	343	1	9
α-helix	344	1
β-strand	351-356	6	9
α-helix	359-360	2
β-strand	368	1	10
β-strand	373-381	9	9
α-helix	384-399	16
α-helix	405-410	6
α-helix	415-435	21

Chain B: 25 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	3-8	6	11
α-helix	10-28	19
β-strand	30	1	12
β-strand	35	1	13
β-strand	36	1	12
α-helix	41-45	5
α-helix	47-49	3
β-strand	51-54	4	13
β-strand	58-61	4	13
β-strand	63-67	5	11
α-helix	70-78	9
α-helix	87-89	3
β-strand	90-92	3	11
α-helix	101-102	2
α-helix	103-107	5
α-helix	108-125	18
β-strand	130-138	9	11
α-helix	143-158	16
β-strand	163-170	8	11
α-helix	171	1
α-helix	173-175	3
α-helix	181-195	15
β-strand	198-203	6	11
α-helix	204-213	10
α-helix	222-236	15
α-helix	238-241	4
α-helix	250-257	8
β-strand	265-266	2	11
β-strand	267-271	5	14
α-helix	286-294	9
α-helix	296-298	3
β-strand	299	1	14
α-helix	305-307	3
β-strand	310-318	9	14
α-helix	323-336	14
α-helix	338-340	3
β-strand	341	1	14
β-strand	349-354	6	14
α-helix	357-358	2
β-strand	364-371	8	14
α-helix	374-390	17
α-helix	395-401	7
α-helix	405-426	22

Chain C: 9 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	3-15	13
α-helix	20-36	17
α-helix	37-40	4
α-helix	43-68	26
β-strand	103-104	2	15
β-strand	107-110	4	16
β-strand	115-121	7	15
β-strand	124-127	4	16
α-helix	134-135	2
β-strand	136-147	12	15
β-strand	150-153	4	16
β-strand	158-169	12	15
β-strand	172-177	6	16
β-strand	183-191	9	15
β-strand	194-199	6	16
α-helix	207	1
β-strand	208-213	6	15
β-strand	216	1	15
β-strand	218-221	4	16
α-helix	222-227	6
β-strand	228-232	5	15
β-strand	248-251	4	16
α-helix	256-258	3
α-helix	260-267	8

Chain D: 69 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	2-16	15
α-helix	20-31	12
α-helix	32-35	4
α-helix	37-40	4
α-helix	44-53	10
α-helix	55-57	3
α-helix	60-83	24
α-helix	91-101	11
α-helix	108-125	18
α-helix	132-143	12
α-helix	152-166	15
α-helix	171-173	3
α-helix	176-179	4
α-helix	182-193	12
α-helix	196-202	7
α-helix	205-217	13
α-helix	224-234	11
α-helix	237-249	13
α-helix	256-276	21
α-helix	278-295	18
α-helix	300-302	3
α-helix	305-320	16
α-helix	326-335	10
α-helix	337-340	4
β-strand	345-347	3	1
β-strand	350-352	3	1
α-helix	354-369	16
α-helix	378-393	16
α-helix	398-414	17
α-helix	416-419	4
α-helix	423-431	9
α-helix	437-451	15
α-helix	459-470	12
α-helix	471-475	5
α-helix	476-478	3
α-helix	483-489	7
α-helix	490-494	5
α-helix	495-499	5
α-helix	505-514	10
α-helix	519-534	16
α-helix	542-552	11
α-helix	571-586	16
α-helix	593-603	11
α-helix	612-625	14
α-helix	631-639	9
α-helix	643-648	6
α-helix	649-651	3
α-helix	655-665	11
α-helix	666-668	3
α-helix	671-684	14
α-helix	685-689	5
α-helix	694-707	14
β-strand	714	1	2
β-strand	717	1	2
α-helix	720-733	14
α-helix	736-740	5
α-helix	742-754	13
α-helix	758-769	12
α-helix	780-790	11
α-helix	795-804	10
α-helix	811-827	17
α-helix	830-842	13
α-helix	845-846	2
α-helix	847-853	7
α-helix	856-859	4
β-strand	860	1	3
α-helix	866	1
β-strand	867	1	3
α-helix	868-870	3
α-helix	871-887	17
α-helix	899-910	12
α-helix	915-935	21
α-helix	942-964	23
α-helix	970-986	17
α-helix	989-993	5

Chain E: 15 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	9-11	3	17
β-strand	14-23	10	17
β-strand	31-37	7	17
α-helix	40-42	3
β-strand	45	1	17
β-strand	48-49	2	18
β-strand	52-53	2	18
β-strand	62-67	6	17
α-helix	68-71	4
β-strand	77	1	17
β-strand	127-128	2	19
α-helix	141-150	10
β-strand	156-158	3	19
β-strand	166	1	20
α-helix	167-175	9
β-strand	182-184	3	19
β-strand	192	1	20
β-strand	207-209	3	19
α-helix	217-226	10
β-strand	232-234	3	19
β-strand	241	1	21
α-helix	242-246	5
α-helix	249-251	3
β-strand	258-260	3	19
β-strand	265	1	21
β-strand	280-282	3	19
β-strand	301-303	3	19
β-strand	311	1	22
α-helix	313-321	9
β-strand	327-329	3	19
β-strand	336	1	22
α-helix	347-356	10
α-helix	371-384	14
α-helix	396-403	8
β-strand	426-431	6	23
α-helix	436-438	3
β-strand	439-444	6	23
β-strand	449	1	24
α-helix	450-460	11
α-helix	465-467	3
β-strand	469-473	5	23
β-strand	479-481	3	23
β-strand	488	1	24
α-helix	489-492	4
β-strand	499-503	5	23

Chain G: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	3-14	12
β-strand	16-23	8	4
α-helix	29-36	8
α-helix	39-41	3
β-strand	53-60	8	4
β-strand	63-70	8	4
α-helix	74-83	10
β-strand	89-95	7	4
α-helix	99-101	3
α-helix	102-115	14
β-strand	120	1	5
β-strand	124	1	5
β-strand	125-131	7	4
α-helix	133-135	3
α-helix	139-156	18
β-strand	163-167	5	4
α-helix	176-189	14

Chain I: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	15-22	8
α-helix	28-41	14
α-helix	47-53	7
α-helix	59-72	14
α-helix	75-77	3
α-helix	78-84	7
α-helix	90-103	14
α-helix	106-108	3
α-helix	109-115	7
α-helix	121-134	14
α-helix	138-148	11
α-helix	152-164	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Chromosome instability protein 1	D	protein	1021	Saccharomyces cerevisiae	P40987 (AlphaFold model)
GTP-binding protein CIN4	G	protein	191	Saccharomyces cerevisiae	P39110 (AlphaFold model)
Tubulin alpha-1A chain	A	protein	451	Sus scrofa	P02550 (AlphaFold model)
Tubulin beta chain	B	protein	445	Sus scrofa	P02554 (AlphaFold model)
Tubulin-specific chaperone C	C	protein	268	Saccharomyces cerevisiae	P46670
iiH5 alphaRep	I	protein	170	Escherichia coli
Protein PAC2	E	protein	421	Saccharomyces cerevisiae	P39937

Sequence of entity 1 (D), FASTA

>9EDR_1 Chromosome instability protein 1 (chains D)
MHHHHHHMNNIRALLDSIQSGVQTVSPEKHQQTIAAINKFQDDPALLDTILPRCVPLLTK
SFFCMSQRDQKLVAELFYNLDKISHSKVLKSLDTSIFRLNEILNYLQDRASPSSFSDVLC
VYLNLSWLSVILLSPYAFKDKFNKTLQVSSRFENYPICIPPINKIKAVLYFKNFTDAFDQ
LPEREQANVPFLNQFLKLFIQSSEKANYYFSNENLRHLQQVALSNDGIKLLPKLFQISFN
HGSHDILDAIVEFFHDHLSSNSTDTRFQLAHSFAKIAKFLHQADPASFIELIDYTIENTV
SLLQAPCDSIDSNELHTSLLIIAEVALAKILPIDLVDRVLTLIIPKTCHFQKSHFQIIKG
HHIRDSTNFIIWSVIRSNRSNSLSPQVLQSLLSHLLINAFFDPELIIRYSSFAALQELLG
RSNKSLALNQNDIALILQANWKDLPRSFEENSGLIRRLFNPENTSKSAVCVWKVFRDWSF
NWNLLENLHLTTMKLNIDYNLVPLIKSKLSSPALLQEVLNKAGSSVTQNCQILYLYLKLF
ENDVNCPKISEICIDIYQKKIKFQLTTQAKRQFNDNSPELFQIFVILKYWQLTGQNDFNQ
ELFWKFVDIVSPQKKLNLYNEFIPIIQQIISQCVSLNYTRIVQLIKSDNELTCRSICHMP
DQEKMCSLFFSQFPLLSPQSRSLLIGELDHHWDVRISLLPSNSYRKFRNIIINCLDDYTI
TQQGDVGRLVRIQALKLMQSHPDFLSGDCDSINPKLTRLLAEPVPEIRKLSYQLLASATS
QITVLSDSSILNFRHKQGLSEEFWKGYAVSAGAIHFTDSQLTSSIDSFIVYYRSLSPSQQ
LELCHDLIRIIPSAKQIAESRIRDRNKDPLTGGMRFDTIKFTIHCVKFWTRIMESGLVVL
HPNFNFQGVFAKFYNLHLLDCTTLRVSVIKFFPFLAISCYHTMRENADQKNLSNIILKRL
LVLVKREYAATKSKFMTDQNVALQGMFQIFLELGVTRQLQALQVACQKHELANILESDIT
L

Sequence of entity 2 (G), FASTA

>9EDR_2 GTP-binding protein CIN4 (chains G)
MGLLSIIRKQKLRDKEIRCLILGLDNSGKSTIVNKLLPKDEQNNDGIMPTVGFQIHSLMI
KDVTISLWDIGGLRTLRPFWDNYFDKTQAMIWCIDVSLSMRFDETLQELKELINRDENRI
GYECAVIVVLNKIDLVEDKSELHRRCLLVESELKCLFKPDIRIELVKCSGVTGEGIDNLR
DRLVESCHFTQ

Sequence of entity 3 (A), FASTA

>9EDR_3 Tubulin alpha-1A chain (chains A)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRAHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYEPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Sequence of entity 4 (B), FASTA

>9EDR_4 Tubulin beta chain (chains B)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATADEQGEFEEEGEEDEA

Sequence of entity 5 (C), FASTA

>9EDR_5 Tubulin-specific chaperone C (chains C)
MDFTAKIKELERELSETSDYKTLQKKTISLRSELNTLSHSLTSYEKEHFSNDIENVLKSI
NAKLSESKGKKRLFSFKQKNSSSAVHKNVERTELANAPAYTTTLKKHYVLEKGDSAFENL
EFCTVTSTTDYSGNSALSGSLCFRNITKCVINLQRIFFQTGSIFITDCTDSIIFLRSPSD
KDFQIRLRDLKNCKILIEKLSPSIDCKQVVIIENCHKCIFNASTRDHLIIQDFSNPFQSE
ETEDNSAFAFEDFDICNKDTMQLFRAYL

Sequence of entity 6 (I), FASTA

>9EDR_6 iiH5 alphaRep (chains I)
MRGSHHHHHHTDPEKVEMYIKNLQDDSPPVRFNAAVALGKIGDERAVEPLIKALKDEDWQ
VRKTAAYALGKIGDERAVEPLIKALKDEDRYVRSRAALALGKIGDERAVEPLIKALKDED
EYVRLSAASALGKIGGERVRAAMEKLAETGTGFARKVAVNYLETHKSLIS

Sequence of entity 7 (E), FASTA

>9EDR_7 Protein PAC2 (chains E)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXQSLVLKIKIRAGKKPSSDLDYWVLPSFTVRYVKSVI
CRKLNFDILNVKLFHENSEGMINEIKYNFRPISDFNVVNGDIIHVSSPVNNKSIQKVNSP
S

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	2

Primary citation

Cryo-EM structures of the tubulin cofactors reveal the molecular basis of alpha/beta-tubulin biogenesis. Taheri, A., Wang, Z., Singal, B. et al. Nat Commun (2025) 17:1405-1405. DOI 10.1038/s41467-025-68142-0 · PubMed

Other PDB entries of the same protein (UniProt P40987 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9EDT 3.7 Å, Tubulin cofactors D,E,G bound to tubulin dimer
9EEB 3.7 Å, Tubulin cofactors D,E,G bound to tubulin dimer
9EDS 3.8 Å, Tubulin cofactors D,E,G,C bound to tubulin dimer -- TBCC N terminus unbound

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