7Z6S: MATCAP

MATCAP bound to a human 14 protofilament microtubule. Determined by electron microscopy at 2.9 Å resolution. Released 11 May 2022.

Method: Electron microscopy
Resolution: 2.9 Å
Organism: Homo sapiens
Chains: 6
Atoms: 19,134
Mol. weight: 313.77 kDa
Ligands: ZN, GDP, MG, GTP
Released: 11 May 2022

Explore 7Z6S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7Z6S contains 154 α-helices and 84 β-strands across 6 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.

Chains A and K: 25 helices, 16 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	65-69	5	1
α-helix	72-80	9
β-strand	93-94	2	1
α-helix	103-104	2
α-helix	105-109	5
α-helix	111-113	3
α-helix	115-127	13
β-strand	134-138	5	1
α-helix	144	1
α-helix	145-149	5
α-helix	150-160	11
β-strand	165-169	5	1
β-strand	171	1	3
α-helix	172-174	3
α-helix	183-194	12
β-strand	200	1	1
β-strand	203	1	4
β-strand	204	1	3
α-helix	206-215	10
α-helix	224-243	20
β-strand	248	1	4
α-helix	252-259	8
α-helix	268	1
β-strand	269-273	5	4
α-helix	288-296	9
α-helix	307-309	3
β-strand	312-321	10	4
α-helix	325-337	13
β-strand	352-356	5	4
α-helix	359-360	2
α-helix	362-363	2
β-strand	373-381	9	4
α-helix	384-400	17
α-helix	405-410	6
α-helix	415-436	22
α-helix	438-440	3

Chain B: 25 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	3-8	6	5
α-helix	10-28	19
β-strand	30	1	6
β-strand	36	1	6
α-helix	42-45	4
α-helix	47-49	3
β-strand	51-54	4	7
β-strand	58-61	4	7
β-strand	63-65	3	5
β-strand	66-67	2	8
α-helix	70-78	9
α-helix	87-89	3
β-strand	91-92	2	8
α-helix	101-102	2
α-helix	103-107	5
α-helix	109-126	18
β-strand	130-138	9	5
α-helix	142	1
α-helix	143-147	5
α-helix	148-158	11
β-strand	163-170	8	5
α-helix	171-172	2
α-helix	181-195	15
β-strand	198-200	3	5
β-strand	202-203	2	5
α-helix	204-209	6
α-helix	210-214	5
α-helix	222-241	20
β-strand	246	1	9
α-helix	250-257	8
β-strand	265-266	2	5
β-strand	267-271	5	9
α-helix	286-293	8
α-helix	296-298	3
α-helix	305-307	3
β-strand	310-317	8	9
α-helix	323-336	14
α-helix	338-340	3
β-strand	341	1	9
β-strand	349-353	5	9
β-strand	365-371	7	9
α-helix	375-390	16
α-helix	395-399	5
α-helix	405-426	22

Chains C and E: 27 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	148-157	10
β-strand	165	1	19
α-helix	172	1
α-helix	174-179	6
α-helix	188-202	15
α-helix	205-213	9
β-strand	216	1	20
α-helix	217-218	2
α-helix	219-233	15
β-strand	240-244	5	21
β-strand	251-256	6	21
β-strand	259-265	7	21
β-strand	270	1	20
α-helix	271-280	10
α-helix	281-286	6
α-helix	287-293	7
α-helix	300-306	7
α-helix	308-310	3
α-helix	314-323	10
α-helix	333-345	13
α-helix	350-356	7
α-helix	357-359	3
α-helix	364-374	11
β-strand	380	1	19
α-helix	388-391	4
α-helix	392-402	11
α-helix	409-414	6
α-helix	420-422	3
α-helix	423-426	4
α-helix	427-429	3
α-helix	435-438	4
α-helix	439-441	3
α-helix	444-457	14
α-helix	462-468	7

Chain H: 25 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	3-8	6	10
α-helix	10-28	19
β-strand	30	1	11
β-strand	36	1	11
α-helix	41-45	5
α-helix	47-49	3
β-strand	51-54	4	12
β-strand	58-61	4	12
β-strand	63-65	3	10
β-strand	66-67	2	13
α-helix	70-78	9
α-helix	87-89	3
β-strand	91-92	2	13
α-helix	101-102	2
α-helix	103-107	5
α-helix	109-126	18
β-strand	130-138	9	10
α-helix	142	1
α-helix	143-147	5
α-helix	148-158	11
β-strand	163-170	8	10
α-helix	171-172	2
α-helix	181-195	15
β-strand	198-200	3	10
β-strand	202-203	2	10
α-helix	204-209	6
α-helix	210-214	5
α-helix	222-241	20
β-strand	246	1	14
α-helix	250-257	8
β-strand	265-266	2	10
β-strand	267-271	5	14
α-helix	286-293	8
α-helix	296-298	3
α-helix	305-307	3
β-strand	310-317	8	14
α-helix	323-336	14
α-helix	338-340	3
β-strand	341	1	14
β-strand	349-353	5	14
β-strand	365-371	7	14
α-helix	375-390	16
α-helix	395-399	5
α-helix	405-426	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tubulin alpha-1B chain	A, K	protein	457	Homo sapiens	P68363 (AlphaFold model)
Tubulin beta-3 chain	B, H	protein	456	Homo sapiens	Q13509 (AlphaFold model)
Uncharacterized protein KIAA0895-like	C, E	protein	471	Homo sapiens	Q68EN5 (AlphaFold model)

Sequence of entity 1 (A, K), FASTA

>7Z6S_1 Tubulin alpha-1B chain (chains A, K)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIHHHHHHGGGDDSFNTFFS
ETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEI
IDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPA
PQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQI
VSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNA
CFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVG
INYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGME
EGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Sequence of entity 2 (B, H), FASTA

>7Z6S_2 Tubulin beta-3 chain (chains B, H)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVYYNEASSHKYV
PRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTARGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVATVFRGRMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRG
LKMSSTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATAEEEGEMYEDDEEESEAQGPKENLYFQ

Sequence of entity 3 (C, E), FASTA

>7Z6S_3 Uncharacterized protein KIAA0895-like (chains C, E)
MVLDSGAQAYDQAPPSPPTSPPSLRHRLKPSDRDGPPLYPWSQSLALPLALAVPPALQPQ
PEQQPFSQMLLGHRGHMRRSESTYSVNSTGRRGRGTLGRPPPGRGRNPGGGTLRPAASLP
HIAKTQRDAGHIASKSPCMLVALRPTNMDRERDKFFQSHYTYNPQFEYQEPMPTAVLEKY
CEASGQFIHQAVGIIEAVLEKFGTYEHFEAATGGQLLTKCQIWSIVRKYMQKEGCAGEVV
VQLSEDLLSQAVMMVENSRPTLAINLTGARQYWLEGMLRHQIGTHYLRGVNNARQPWHNA
EGRLRYGLRPANPTEEGLASLHSVLFRKQPFLWRAALLYYTIHRAARMSFRQLFQDLERY
VQDADVRWEYCVRAKRGQTDTSLPGCFSKDQVYLDGIVRILRHRQTIDFPLLTSLGKVSY
EDVDHLRPHGVLDNTRVPHFMQDLARYRQQLEHIMATNRLDEAELGRLLPD

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	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

Posttranslational modification of microtubules by the MATCAP detyrosinase. Landskron, L., Bak, J., Adamopoulos, A. et al. Science (2022) 376:eabn6020-eabn6020. DOI 10.1126/science.abn6020 · 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.
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
7M18 3.38 Å, HeLa-tubulin in complex with cryptophycin 1

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