6HC2: NuMA/LGN hetero-hexamers

Crystal structure of NuMA/LGN hetero-hexamers. Determined by X-ray diffraction at 4.31 Å resolution. Released 29 May 2019.

Method: X-ray diffraction
Resolution: 4.31 Å
Organism: Homo sapiens
Chains: 24
Atoms: 37,558
Mol. weight: 582.04 kDa
Released: 29 May 2019

Explore 6HC2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6HC2 contains 229 α-helices and 2 β-strands across 22 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: 17 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	17-30	14
α-helix	33-46	14
β-strand	48	1	1
α-helix	51-67	17
α-helix	71-87	17
α-helix	91-108	18
α-helix	111-127	17
α-helix	131-150	20
α-helix	165-188	24
α-helix	191-208	18
α-helix	211-228	18
α-helix	231-248	18
α-helix	251-267	17
α-helix	271-287	17
α-helix	291-307	17
α-helix	311-328	18
α-helix	331-348	18
α-helix	351-365	15

Chains C, I and S: 17 helices, 0 β-strands

Element	Residues	Length
α-helix	17-30	14
α-helix	33-46	14
α-helix	51-67	17
α-helix	71-87	17
α-helix	91-107	17
α-helix	111-127	17
α-helix	131-150	20
α-helix	165-188	24
α-helix	191-208	18
α-helix	211-228	18
α-helix	231-248	18
α-helix	251-267	17
α-helix	271-287	17
α-helix	291-307	17
α-helix	311-328	18
α-helix	331-348	18
α-helix	351-366	16

Chain D: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1870-1872	3
α-helix	1910-1912	3

Chains E and U: 17 helices, 0 β-strands

Element	Residues	Length
α-helix	17-30	14
α-helix	33-46	14
α-helix	51-67	17
α-helix	71-87	17
α-helix	91-107	17
α-helix	111-127	17
α-helix	131-150	20
α-helix	165-188	24
α-helix	191-208	18
α-helix	211-228	18
α-helix	231-248	18
α-helix	251-267	17
α-helix	271-287	17
α-helix	291-307	17
α-helix	311-328	18
α-helix	331-348	18
α-helix	351-365	15

Chain F: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	1876	1	1
α-helix	1910-1912	3
α-helix	1919-1923	5

Chain G: 17 helices, 0 β-strands

Element	Residues	Length
α-helix	17-30	14
α-helix	33-46	14
α-helix	51-67	17
α-helix	71-87	17
α-helix	91-107	17
α-helix	111-127	17
α-helix	131-150	20
α-helix	164-188	25
α-helix	191-208	18
α-helix	211-228	18
α-helix	231-248	18
α-helix	251-267	17
α-helix	271-287	17
α-helix	291-307	17
α-helix	311-328	18
α-helix	331-348	18
α-helix	351-366	16

Chains H and N: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1910-1912	3
α-helix	1919-1922	4

Chain K: 18 helices, 0 β-strands

Element	Residues	Length
α-helix	9-13	5
α-helix	17-30	14
α-helix	33-46	14
α-helix	51-67	17
α-helix	71-87	17
α-helix	91-107	17
α-helix	111-127	17
α-helix	131-150	20
α-helix	166-188	23
α-helix	191-208	18
α-helix	211-228	18
α-helix	231-248	18
α-helix	251-267	17
α-helix	271-287	17
α-helix	291-307	17
α-helix	311-328	18
α-helix	331-348	18
α-helix	351-366	16

9 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
G-protein-signaling modulator 2	A, C, E, G, I, K, M, O, Q, S, U, W	protein	367	Homo sapiens	P81274 (AlphaFold model)
Nuclear mitotic apparatus protein 1	B, D, F, H, J, L, N, P, R, T, V, X	protein	71	Homo sapiens	Q14980 (AlphaFold model)

Sequence of entity 1 (A, C, E, G, I, K, M, O, Q, S, U, W), FASTA

>6HC2_1 G-protein-signaling modulator 2 (chains A, C, E, G, I, K, M, O, Q, S, U, W)
GPLGSMFHVRYRMEASCLELALEGERLCKSGDCRAGVSFFEAAVQVGTEDLKTLSAIYSQ
LGNAYFYLHDYAKALEYHHHDLTLARTIGDQLGEAKASGNLGNTLKVLGNFDEAIVCCQR
HLDISRELNDKVGEARALYNLGNVYHAKGKSFGCPGPQDVGEFPEEVRDALQAAVDFYEE
NLSLVTALGDRAAQGRAFGNLGNTHYLLGNFRDAVIAHEQRLLIAKEFGDKAAERRAYSN
LGNAYIFLGEFETASEYYKKTLLLARQLKDRAVEAQSCYSLGNTYTLLQDYEKAIDYHLK
HLAIAQELNDRIGEGRACWSLGNAYTALGNHDQAMHFAEKHLEISREVGDKSGELTARLN
LSDLQMV

Sequence of entity 2 (B, D, F, H, J, L, N, P, R, T, V, X), FASTA

>6HC2_2 Nuclear mitotic apparatus protein 1 (chains B, D, F, H, J, L, N, P, R, T, V, X)
GPLGSPDYGNSALLSLPGYRPTTRSSARRSQAGVSSGAPPGRNSFYMGTCQDEPEQLDDW
NRIAELQQRNR

Primary citation

Hexameric NuMA:LGN structures promote multivalent interactions required for planar epithelial divisions. Pirovano, L., Culurgioni, S., Carminati, M. et al. Nat Commun (2019) 10:2208-2208. DOI 10.1038/s41467-019-09999-w · PubMed

Other PDB entries of the same protein (UniProt P81274 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4WND 1.5 Å, Crystal structure of the TPR domain of LGN in complex with Frmpd4/Preso1 at 1.5 Angstrom…
4WNE 2.0 Å, Crystal structure of the TPR domain of LGN in complex with Frmpd4/Preso1 at 2.0 Angstrom…
4WNG 2.11 Å, Crystal structure of the TPR domain of LGN in complex with Frmpd4/Preso1 at 2.1 Angstrom…
3SF4 2.6 Å, Crystal structure of the complex between the conserved cell polarity proteins…
4WNF 2.9 Å, Crystal structure of the oxidized TPR domain of LGN in complex with Frmpd4/Preso1 at 2.9…
5A6C 2.9 Å, Concomitant binding of Afadin to LGN and F-actin directs planar spindle orientation

Browse structure collections

About this viewer

MolViewer shows 6HC2 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.