7MW0: Homo sapiens NUP93 solenoid

Crystal structure of Homo sapiens NUP93 solenoid (residues 174-819). Determined by X-ray diffraction at 2.0 Å resolution. Released 15 Jun 2022.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 1
Atoms: 5,258
Mol. weight: 76.89 kDa
Released: 15 Jun 2022

Explore 7MW0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7MW0 contains 43 α-helices and 11 β-strands across 1 chain. 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: 43 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	180-197	18
α-helix	200-204	5
α-helix	205-210	6
α-helix	211-215	5
α-helix	218-230	13
α-helix	241-246	6
α-helix	248-275	28
α-helix	289-300	12
β-strand	312-313	2	1
β-strand	316-317	2	1
α-helix	318-327	10
α-helix	331-339	9
α-helix	342-345	4
α-helix	348-357	10
α-helix	365-374	10
α-helix	375-379	5
α-helix	385-394	10
α-helix	410-420	11
β-strand	421-422	2	2
β-strand	435-436	2	2
α-helix	437-442	6
α-helix	443-448	6
α-helix	449-452	4
α-helix	459-468	10
α-helix	472-481	10
α-helix	483-485	3
α-helix	486-498	13
β-strand	504	1	3
β-strand	513-514	2	3
α-helix	520	1
β-strand	525-526	2	3
α-helix	528-536	9
α-helix	544-551	8
α-helix	552-554	3
β-strand	558	1	4
β-strand	564	1	4
α-helix	565-577	13
α-helix	580-584	5
β-strand	586-587	2	5
β-strand	593-594	2	5
α-helix	597-601	5
α-helix	606-618	13
α-helix	622-631	10
α-helix	635-646	12
α-helix	647-649	3
α-helix	659-677	19
α-helix	683-703	21
α-helix	707-717	11
α-helix	724-726	3
α-helix	727-734	8
α-helix	739-742	4
α-helix	745-761	17
α-helix	781-797	17
α-helix	804-816	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Nuclear pore complex protein Nup93	A	protein	672	Homo sapiens	Q8N1F7 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>7MW0_1 Nuclear pore complex protein Nup93 (chains A)
SSGLNDIFEAQKIEWHEGSAGGSGGSGRSSLDNIEMAYARQIYIYNEKIVNGHLQPNLVD
LCASVAELDDKSISDMWTMVKQMTDVLLTPATDALKNRSSVEVRMEFVRQALAYLEQSYK
NYTLVTVFGNLHQAQLGGVPGTYQLVRSFLNIKLPAPLPGLQDGEVEGHPVWALIYYCMR
CGDLLAASQVVNRAQHQLGEFKTWFQEYMNSKDRRLSPATENKLRLHYRRALRNNTDPYK
RAVYCIIGRCDVTDNQSEVADKTEDYLWLKLNQVCFDDDGTSSPQDRLTLSQFQKQLLED
YGESHFTVNQQPFLYFQVLFLTAQFEAAVAFLFRMERLRCHAVHVALVLFELKLLLKSSG
QSAQLLSHEPGDPPCLRRLNFVRLLMLYTRKFESTDPREALQYFYFLRDEKDSQGENMFL
RCVSELVIESREFDMILGKLENDGSRKPGVIDKFTSDTKPIINKVASVAENKGLFEEAAK
LYDLAKNADKVLELMNKLLSPVVPQISAPQSNKERLKNMALSIAERYRAQGISANKFVDS
TFYLLLDLITFFDEYHSGHIDRAFDIIERLKLVPLNQESVEERVAAFRNFSDEIRHNLSE
VLLATMNILFTQFKRLKGTSPSSSSRPQRVIEDRDSQLRSQARTLITFAGMIPYRTSGDT
NARLVQMEVLMN

Primary citation

Architecture of the linker-scaffold in the nuclear pore. Petrovic, S., Samanta, D., Perriches, T. et al. Science (2022) 376:eabm9798-eabm9798. DOI 10.1126/science.abm9798 · PubMed

Other PDB entries of the same protein (UniProt Q8N1F7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7MW1 3.4 Å, Crystal structure of the Homo sapiens NUP93-NUP53 complex (NUP93 residues 174-819; NUP53…
7R5K 12.0 Å, Human nuclear pore complex (constricted)
5IJN 21.4 Å, Composite structure of the inner ring of the human nuclear pore complex (32 copies of…
5IJO 21.4 Å, Alternative composite structure of the inner ring of the human nuclear pore complex (16…
7PER 35.0 Å, Model of the inner ring of the human nuclear pore complex
7R5J 50.0 Å, Human nuclear pore complex (dilated)
9A25 Molecular assembly pathway of the human Nuclear Pore Complex after cell division
9A8T Integrative spatiotemporal modeling of biomolecular processes: application to the…

Browse structure collections

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