8FZK: Dimeric human importin alpha subunit

Dimeric human importin alpha subunit. Determined by X-ray diffraction at 2.1 Å resolution. Released 8 Feb 2023.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 4
Atoms: 13,375
Mol. weight: 199.39 kDa
Ligands: MG
Released: 8 Feb 2023

Explore 8FZK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8FZK contains 128 α-helices and 0 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: 32 helices, 0 β-strands

Element	Residues	Length
α-helix	80-85	6
α-helix	90-105	16
α-helix	112-118	7
α-helix	121-127	7
α-helix	134-148	15
α-helix	152-160	9
α-helix	163-171	9
α-helix	176-192	17
α-helix	194-202	9
α-helix	206-212	7
α-helix	218-220	3
α-helix	223-237	15
α-helix	243-245	3
α-helix	246-259	14
α-helix	265-279	15
α-helix	283-291	9
α-helix	295-302	8
α-helix	307-320	14
α-helix	325-333	9
α-helix	336-339	4
α-helix	340-343	4
α-helix	349-362	14
α-helix	367-375	9
α-helix	379-388	10
α-helix	391-407	17
α-helix	410-418	9
α-helix	422-427	6
α-helix	428-430	3
α-helix	434-454	21
α-helix	457-466	10
α-helix	469-475	7
α-helix	482-495	14

Chain B: 32 helices, 0 β-strands

Element	Residues	Length
α-helix	78-85	8
α-helix	90-105	16
α-helix	112-117	6
α-helix	120-128	9
α-helix	134-148	15
α-helix	152-160	9
α-helix	163-171	9
α-helix	176-191	16
α-helix	194-202	9
α-helix	206-211	6
α-helix	218-220	3
α-helix	223-237	15
α-helix	243-245	3
α-helix	246-259	14
α-helix	265-279	15
α-helix	283-291	9
α-helix	295-302	8
α-helix	307-320	14
α-helix	325-333	9
α-helix	336-339	4
α-helix	340-343	4
α-helix	349-363	15
α-helix	367-375	9
α-helix	378-388	11
α-helix	391-407	17
α-helix	410-418	9
α-helix	422-427	6
α-helix	428-430	3
α-helix	434-454	21
α-helix	457-466	10
α-helix	469-475	7
α-helix	482-495	14

Chain C: 32 helices, 0 β-strands

Element	Residues	Length
α-helix	78-85	8
α-helix	90-105	16
α-helix	112-117	6
α-helix	120-127	8
α-helix	134-148	15
α-helix	152-160	9
α-helix	163-170	8
α-helix	176-190	15
α-helix	194-202	9
α-helix	206-211	6
α-helix	218-220	3
α-helix	223-236	14
α-helix	243-245	3
α-helix	246-259	14
α-helix	265-278	14
α-helix	283-290	8
α-helix	295-301	7
α-helix	307-320	14
α-helix	325-333	9
α-helix	336-339	4
α-helix	340-343	4
α-helix	349-363	15
α-helix	367-375	9
α-helix	378-388	11
α-helix	391-407	17
α-helix	410-418	9
α-helix	422-427	6
α-helix	428-430	3
α-helix	434-454	21
α-helix	457-466	10
α-helix	469-475	7
α-helix	482-495	14

Chain D: 32 helices, 0 β-strands

Element	Residues	Length
α-helix	78-85	8
α-helix	90-105	16
α-helix	112-117	6
α-helix	120-128	9
α-helix	134-148	15
α-helix	152-160	9
α-helix	163-170	8
α-helix	176-191	16
α-helix	194-202	9
α-helix	206-211	6
α-helix	218-220	3
α-helix	223-237	15
α-helix	243-245	3
α-helix	246-259	14
α-helix	265-279	15
α-helix	283-290	8
α-helix	295-302	8
α-helix	307-320	14
α-helix	325-333	9
α-helix	336-339	4
α-helix	340-343	4
α-helix	349-363	15
α-helix	367-375	9
α-helix	378-388	11
α-helix	391-407	17
α-helix	410-418	9
α-helix	422-427	6
α-helix	428-430	3
α-helix	434-454	21
α-helix	457-466	10
α-helix	469-475	7
α-helix	482-495	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Importin subunit alpha-1	A, B, C, D	protein	460	Homo sapiens	P52292 (AlphaFold model)

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

>8FZK_1 Importin subunit alpha-1 (chains A, B, C, D)
SQGTVNWSVDDIVKGINSSNVENQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLG
RTDCSPIQFESAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNI
AGDGSVFRDLVIKYGAVDPLLALLAVPDMSSLACGYLRNLTWTLSNLCRNKNPAPPIDAV
EQILPTLVRLLHHDDPEVLADTCWAISYLTDGPNERIGMVVKTGVVPQLVKLLGASELPI
VTPALRAIGNIVTGTDEQTQVVIDAGALAVFPSLLTNPKTNIQKEATWTMSNITAGRQDQ
IQQVVNHGLVPFLVSVLSKADFKTQKEAVWAVTNYTSGGTVEQIVYLVHCGIIEPLMNLL
TAKDTKIILVILDAISNIFQAAEKLGETEKLSIMIEECGGLDKIEALQNHENESVYKASL
SLIEKYFSVEEEEDQNVVPETTSEGYTFQVQDGAPGTFNF

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1

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

Primary citation

Dimeric human importin alpha subunit. Donnelly, C.M., Stewart, M., Forwood, J.K. To be published.

Other PDB entries of the same protein (UniProt P52292 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4WV6 1.75 Å, Heterodimer of Importin alpha 1 with nuclear localization signal of TAF8
3FEY 2.2 Å, Crystal structure of the CBC-importin alpha complex.
7N9H 2.2 Å, Structure of the mammalian importin a1 bound to the TDP-43 NLS
1QGR 2.3 Å, Structure of importin beta bound to the ibb domain of importin alpha (II crystal form,…
5H43 2.3 Å, Structural and mechanistical studies of the nuclear import by Importin-alpha
1QGK 2.5 Å, Structure of importin beta bound to the ibb domain of importin alpha
4E4V 2.53 Å, The crystal structure of the dimeric human importin alpha 1 at 2.5 angstrom resolution.
3WPT 2.63 Å, Crystal structure of closed dimer of human importin-alpha1 (Rch1)
7CRU 2.8 Å, hnRNPK NLS in complex with Importin alpha 1 (KPNA2)
1EFX 3.0 Å, Structure of a complex between the human natural killer cell receptor KIR2DL2 and a…
7N8J 3.2 Å, Human importin alpha 1 in complex with Bimax2 peptide
9BFC 3.2 Å, Cryo-EM structure of importin alpha-1/beta bound to FG repeats

Browse structure collections

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