6QJA: Nuclear mitotic apparatus protein 1

Organizational principles of the NuMA-Dynein interaction interface and implications for mitotic spindle functions. Determined by X-ray diffraction at 1.54 Å resolution. Released 5 Feb 2020.

Method: X-ray diffraction
Resolution: 1.54 Å
Organism: Homo sapiens
Chains: 4
Atoms: 5,244
Mol. weight: 71.34 kDa
Ligands: MG
Released: 5 Feb 2020

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

Secondary structure: helices and β-sheets

6QJA contains 41 α-helices and 4 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: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	-2-1	4
α-helix	5-17	13
α-helix	27-30	4
α-helix	34-44	11
α-helix	48-52	5
α-helix	57-70	14
α-helix	84-88	5
α-helix	92-107	16
α-helix	112-114	3
α-helix	116-118	3
α-helix	121-137	17
α-helix	143-152	10

Chain B: 9 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	1
α-helix	5-17	13
α-helix	27-30	4
α-helix	34-44	11
α-helix	48-52	5
α-helix	57-70	14
α-helix	84-88	5
α-helix	92-107	16
α-helix	121-137	17
α-helix	143-151	9
β-strand	152	1	1

Chain C: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	27-30	4
α-helix	34-44	11
α-helix	57-70	14
α-helix	84-88	5
α-helix	92-108	17
α-helix	116-118	3
α-helix	121-137	17
α-helix	143-151	9

Chain D: 11 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	3	1	2
α-helix	5-17	13
α-helix	27-30	4
α-helix	34-44	11
α-helix	48-52	5
α-helix	57-71	15
α-helix	75-77	3
α-helix	84-88	5
α-helix	92-109	18
α-helix	113-114	2
α-helix	121-136	16
α-helix	143-151	9
β-strand	152	1	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Nuclear mitotic apparatus protein 1	A, B, C, D	protein	157	Homo sapiens	Q14980 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>6QJA_1 Nuclear mitotic apparatus protein 1 (chains A, B, C, D)
GPMGMTLHATRGAALLSWVNSLHVADPVEAVLQLQDCSIFIKIIDRIHGTEEGQQILKQP
VSERLDFVCSFLQKNRKHPSSPECLVSAQKVLEGSELELAKMTMLLLYHSTMSSKSPRDW
EQFEYKIQAELAVILKFVLDHEDGLNLNEDLENFLQK

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1

Water and common crystallization additives (CL) are not listed.

Primary citation

Organizational Principles of the NuMA-Dynein Interaction Interface and Implications for Mitotic Spindle Functions. Renna, C., Rizzelli, F., Carminati, M. et al. Structure (2020) 28:820-829.e6. DOI 10.1016/j.str.2020.04.017 · PubMed

Other PDB entries of the same protein (UniProt Q14980 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3RO2 2.3 Å, Structures of the LGN/NuMA complex
5GXW 2.39 Å, Importin and NuMA complex
6HC2 4.31 Å, Crystal structure of NuMA/LGN hetero-hexamers
9HHL 6.53 Å, Structure of Dynein-Dynactin-NuMA-LIS1

Browse structure collections

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