6XF1: Nesprin-2

Nesprin-2G(aa1425-1649)-FHOD1(aa1-339) complex, H. sapiens. Determined by X-ray diffraction at 2.8 Å resolution. Released 3 Feb 2021.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 8,580
Mol. weight: 125.05 kDa
Released: 3 Feb 2021

Explore 6XF1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6XF1 contains 62 α-helices and 13 β-strands across 4 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: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	1422-1451	30
α-helix	1460-1492	33
α-helix	1501-1556	56
α-helix	1562-1564	3
α-helix	1567-1586	20
α-helix	1588-1606	19
α-helix	1617-1646	30

Chain B: 23 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	21-22	2	1
α-helix	28-30	3
β-strand	36	1	1
α-helix	40-42	3
β-strand	50	1	2
α-helix	55-62	8
α-helix	68-70	3
β-strand	71-74	4	1
α-helix	80	1
β-strand	81	1	1
α-helix	82-83	2
β-strand	86	1	2
α-helix	87-93	7
α-helix	99-103	5
β-strand	111-114	4	1
α-helix	116-129	14
α-helix	132-148	17
α-helix	152-158	7
α-helix	161-169	9
α-helix	174-189	16
α-helix	191-199	9
α-helix	201-210	10
α-helix	216-232	17
α-helix	237-251	15
α-helix	254	1
α-helix	257-263	7
α-helix	271-285	15
α-helix	291-303	13
α-helix	306-315	10
α-helix	321-333	13

Chain C: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	1425-1451	27
α-helix	1460-1479	20
α-helix	1481-1492	12
α-helix	1502-1555	54
α-helix	1562-1564	3
α-helix	1567-1586	20
α-helix	1588-1606	19
α-helix	1617-1646	30

Chain D: 24 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	17-22	6	3
β-strand	36	1	3
α-helix	40-41	2
β-strand	42-44	3	3
α-helix	52-54	3
α-helix	55-62	8
α-helix	68-70	3
β-strand	71-75	5	3
α-helix	80	1
β-strand	81	1	3
α-helix	82-83	2
α-helix	92-94	3
α-helix	96-103	8
β-strand	109-114	6	3
α-helix	116-129	14
α-helix	133-148	16
α-helix	152-158	7
α-helix	161-169	9
α-helix	174-188	15
α-helix	191-199	9
α-helix	201-209	9
α-helix	210-212	3
α-helix	216-232	17
α-helix	237-251	15
α-helix	254	1
α-helix	257-263	7
α-helix	271-285	15
α-helix	291-304	14
α-helix	306-315	10
α-helix	321-333	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Nesprin-2	A, C	protein	230	Homo sapiens	Q8WXH0 (AlphaFold model)
FH1/FH2 domain-containing protein 1	B, D	protein	321	Homo sapiens	Q9Y613 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>6XF1_1 Nesprin-2 (chains A, C)
PGSEDENKLLEACIFKNNELLKNIQDVQSQISKIGLKDPTVPAVKHRKKSLIRLDKVLDE
YEEEKRHLQEMANSLPHFKDGREKTVNQQCQNTVVLWENTKALVTECLEQCGRVLELLKQ
YQNFKSILTTLIQKEESVISLQASYMGKENLKKRIAEIEIVKEEFNEHLEVVDKINQVCK
NLQFYLNKMKTFEEPPFEKEANIIVDRWLDINEKTEDYYENLGRALALWD

Sequence of entity 2 (B, D), FASTA

>6XF1_2 FH1/FH2 domain-containing protein 1 (chains B, D)
SVVTVRVQYLEDTDPFACANFPEPRRAPTCSLDGALPLGAQIPAVHRLLGAPLKLEDCAL
QVSPSGYYLDTELSLEEQREMLEGFYEEISKGRKPTLILRTQLSVRVNAILEKLYSSSGP
ELRRSLFSLKQIFQEDKDLVPEFVHSEGLSCLIRVGAAADHNYQSYILRALGQLMLFVDG
MLGVVAHSDTIQWLYTLCASLSRLVVKTALKLLLVFVEYSENNAPLFIRAVNSVASTTGA
PPWANLVSILEEKNGADPELLVYTVTLINKTLAALPDQDSFYDVTDALEQQGMEALVQRH
LGTAGTDVDLRTQLVLYENAL

Primary citation

Structures of FHOD1-Nesprin1/2 complexes reveal alternate binding modes for the FH3 domain of formins. Lim, S.M., Cruz, V.E., Antoku, S. et al. Structure (2021) 29:540-552.e5. DOI 10.1016/j.str.2020.12.013 · PubMed

Other PDB entries of the same protein (UniProt Q8WXH0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4DXS 2.71 Å, Human SUN2-KASH2 complex
4FI9 3.05 Å, Structure of human SUN-KASH complex

Browse structure collections

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