1BK5: Karyopherin alpha from saccharomyces cerevisiae

Karyopherin alpha from saccharomyces cerevisiae. Determined by X-ray diffraction at 2.2 Å resolution. Released 6 Jan 1999.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Saccharomyces cerevisiae
Chains: 2
Atoms: 6,782
Mol. weight: 93.55 kDa
Ligands: CO
Released: 6 Jan 1999

Explore 1BK5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1BK5 contains 66 α-helices and 0 β-strands across 2 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: 33 helices, 0 β-strands

Element	Residues	Length
α-helix	90-96	7
α-helix	101-114	14
α-helix	123-128	6
α-helix	132-137	6
α-helix	145-159	15
α-helix	163-171	9
α-helix	175-184	10
α-helix	187-203	17
α-helix	205-213	9
α-helix	217-222	6
α-helix	223-225	3
α-helix	229-243	15
α-helix	249-250	2
α-helix	252-255	4
α-helix	256-258	3
α-helix	259-265	7
α-helix	271-284	14
α-helix	289-297	9
α-helix	301-307	7
α-helix	313-326	14
α-helix	331-339	9
α-helix	342-349	8
α-helix	355-369	15
α-helix	373-381	9
α-helix	385-394	10
α-helix	397-412	16
α-helix	418-426	9
α-helix	430-439	10
α-helix	442-465	24
α-helix	472-480	9
α-helix	482-488	7
α-helix	489-491	3
α-helix	495-508	14

Chain B: 33 helices, 0 β-strands

Element	Residues	Length
α-helix	90-96	7
α-helix	101-114	14
α-helix	123-128	6
α-helix	132-137	6
α-helix	145-159	15
α-helix	163-171	9
α-helix	175-184	10
α-helix	187-201	15
α-helix	205-213	9
α-helix	217-222	6
α-helix	223-225	3
α-helix	229-243	15
α-helix	252-255	4
α-helix	256-258	3
α-helix	259-265	7
α-helix	271-284	14
α-helix	289-297	9
α-helix	301-306	6
α-helix	307-309	3
α-helix	313-326	14
α-helix	331-339	9
α-helix	342-349	8
α-helix	355-369	15
α-helix	373-381	9
α-helix	385-394	10
α-helix	397-412	16
α-helix	418-426	9
α-helix	430-439	10
α-helix	442-464	23
α-helix	472-479	8
α-helix	482-488	7
α-helix	489-491	3
α-helix	495-508	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Karyopherin alpha	A, B	protein	422	Saccharomyces cerevisiae	Q02821 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1BK5_1 KARYOPHERIN ALPHA (chains A, B)
LPQMTQQLNSDDMQEQLSATVKFRQILSREHRPPIDVVIQAGVVPRLVEFMRENQPEMLQ
LEAAWALTNIASGTSAQTKVVVDADAVPLFIQLLYTGSVEVKEQAIWALGNVAGDSTDYR
DYVLQCNAMEPILGLFNSNKPSLIRTATWTLSNLCRGKKPQPDWSVVSQALPTLAKLIYS
MDTETLVDACWAISYLSDGPQEAIQAVIDVRIPKRLVELLSHESTLVQTPALRAVGNIVT
GNDLQTQVVINAGVLPALRLLLSSPKENIKKEACWTISNITAGNTEQIQAVIDANLIPPL
VKLLEVAEYKTKKEACWAISNASSGGLQRPDIIRYLVSQGCIKPLCDLLEIADNRIIEVT
LDALENILKMGEADKEARGLNINENADFIEKAGGMEKIFNCQQNENDKIYEKAYKIIETY
FG

Ligands and cofactors

ID	Name	Formula	Copies
CO	Cobalt (II) ion	Co	2

Primary citation

Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha. Conti, E., Uy, M., Leighton, L. et al. Cell (1998) 94:193-204. DOI 10.1016/S0092-8674(00)81419-1 · PubMed

Other PDB entries of the same protein (UniProt Q02821 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1WA5 2.0 Å, Structure of the Cse1:Imp-alpha:RanGTP complex
1EE4 2.1 Å, Crystal structure of yeast karyopherin (importin) alpha in a complex with a C-myc nls…
5H2X 2.2 Å, Crystal structure of the karyopherin Kap60p bound to the SUMO protease Ulp1p (150-172)
4XZR 2.25 Å, Structure of yeast importin a bound to the membrane protein Nuclear Localization Signal…
1EE5 2.4 Å, Yeast karyopherin (importin) alpha in a complex with a nucleoplasmin nls peptide
4PVZ 2.5 Å, Structure of yeast importin a bound to the membrane protein Nuclear Localization Signal…
5H2W 2.5 Å, Crystal structure of the karyopherin Kap60p bound to the SUMO protease Ulp1p (150-340)
1UN0 2.6 Å, Crystal Structure of Yeast Karyopherin (Importin) alpha in complex with a Nup2p…
2C1T 2.6 Å, Structure of the Kap60p:Nup2 complex
5T94 2.63 Å, Crystal structure of Kap60 bound to yeast RCC1 (Prp20)
1BK6 2.8 Å, Karyopherin alpha (YEAST) + SV40 T antigen nls

Browse structure collections

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