3LWW: Importin subunit beta-1

Structure of an open and closed conformation of Human Importin Beta bound to the Snurportin1 IBB-domain trapped in the same crystallographic asymmetric unit. Determined by X-ray diffraction at 3.15 Å resolution. Released 2 Jun 2010.

Method: X-ray diffraction
Resolution: 3.15 Å
Organism: Homo sapiens
Chains: 4
Atoms: 14,127
Mol. weight: 204.57 kDa
Released: 2 Jun 2010

Explore 3LWW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3LWW contains 111 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: 51 helices, 0 β-strands

Element	Residues	Length
α-helix	3-8	6
α-helix	15-31	17
α-helix	33-45	13
α-helix	51-63	13
α-helix	70-82	13
α-helix	85-98	14
α-helix	108-120	13
α-helix	129-138	10
α-helix	144-160	17
α-helix	170-181	12
α-helix	188-201	14
α-helix	206-209	4
α-helix	212-225	14
α-helix	231-247	17
α-helix	250-252	3
α-helix	256-260	5
α-helix	261-269	9
α-helix	273-300	28
α-helix	314-317	4
α-helix	319-329	11
α-helix	344-358	15
α-helix	364-372	9
α-helix	381-392	12
α-helix	399-416	18
α-helix	422-438	17
α-helix	440-443	4
α-helix	449-459	11
α-helix	464-481	18
α-helix	498-501	4
α-helix	503-513	11
α-helix	521-523	3
α-helix	524-537	14
α-helix	544-561	18
α-helix	578-592	15
α-helix	599-613	15
α-helix	628-635	8
α-helix	650-657	8
α-helix	667-677	11
α-helix	686-688	3
α-helix	690-696	7
α-helix	711-715	5
α-helix	728-730	3
α-helix	732-744	13
α-helix	755-758	4
α-helix	762-775	14
α-helix	788-790	3
α-helix	791-806	16
α-helix	812-828	17
α-helix	841-843	3
α-helix	844-851	8
α-helix	859-869	11

Chain B: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	27-30	4
α-helix	40-58	19
α-helix	59-61	3

Chain C: 56 helices, 0 β-strands

Element	Residues	Length
α-helix	3-8	6
α-helix	9-11	3
α-helix	15-25	11
α-helix	33-45	13
α-helix	51-65	15
α-helix	70-81	12
α-helix	85-98	14
α-helix	109-120	12
α-helix	121-123	3
α-helix	130-138	9
α-helix	144-160	17
α-helix	170-181	12
α-helix	188-199	12
α-helix	202-204	3
α-helix	206-210	5
α-helix	212-226	15
α-helix	231-247	17
α-helix	249-251	3
α-helix	256-260	5
α-helix	261-268	8
α-helix	273-290	18
α-helix	298-301	4
α-helix	305-307	3
α-helix	314-329	16
α-helix	344-358	15
α-helix	364-373	10
α-helix	380-392	13
α-helix	399-401	3
α-helix	403-417	15
α-helix	422-438	17
α-helix	449-453	5
α-helix	454-456	3
α-helix	469-483	15
α-helix	499-502	4
α-helix	504-506	3
α-helix	528-533	6
α-helix	548-561	14
α-helix	580-584	5
α-helix	600-618	19
α-helix	626-639	14
α-helix	640-643	4
α-helix	644-659	16
α-helix	664-681	18
α-helix	686-688	3
α-helix	689-700	12
α-helix	709-724	16
α-helix	725-730	6
α-helix	732-744	13
α-helix	755-777	23
α-helix	787-789	3
α-helix	791-793	3
α-helix	794-805	12
α-helix	812-829	18
α-helix	832-839	8
α-helix	841-850	10
α-helix	859-870	12

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	40-63	24

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Importin subunit beta-1	A, C	protein	876	Homo sapiens	Q14974 (AlphaFold model)
Snurportin-1	B, D	protein	40		O95149 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>3LWW_1 Importin subunit beta-1 (chains A, C)
MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQ
IKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAE
IPVNQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQG
MRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQN
LVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEA
AEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLATCCE
DDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGCILEGPEPSQLKPLVIQAMPTLIELMKDP
SVVVRDTAAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEA
AYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSA
KDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDA
LQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKN
YAEYQVCLAAVGLVGDLCRALQSNIIPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDI
ALAIGGEFKKYLEVVLNTLQQASQAQVDKSDYDMVDYLNELRESCLEAYTGIVQGLKGDQ
ENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEAR
PMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA

Sequence of entity 2 (B, D), FASTA

>3LWW_2 Snurportin-1 (chains B, D)
HPRLSQYKSKYSSLEQSERRRRLLELQKSKRLDYVNHARR

Primary citation

Conformational selection in the recognition of the snurportin importin beta binding domain by importin beta. Bhardwaj, A., Cingolani, G. Biochemistry (2010) 49:5042-5047. DOI 10.1021/bi100292y · PubMed

Other PDB entries of the same protein (UniProt Q14974 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1IBR 2.3 Å, Complex of ran with importin beta
1QGR 2.3 Å, Structure of importin beta bound to the ibb domain of importin alpha (II crystal form,…
2P8Q 2.35 Å, Crystal Structure of human Importin beta bound to the Snurportin1 IBB-domain
1QGK 2.5 Å, Structure of importin beta bound to the ibb domain of importin alpha
3W5K 2.6 Å, Crystal structure of Snail1 and importin beta complex
9N85 2.6 Å, Cryo-EM structure of human importin beta:Ran-GTP:RanBP1 trimeric complex
1F59 2.8 Å, Importin-beta-fxfg nucleoporin complex
1O6O 2.8 Å, Importin Beta aa1-442 bound to five FxFG repeats from yeast Nsp1p. Second crystal form
1O6P 2.8 Å, Importin Beta bound to a GLFG Nucleoporin peptide
2QNA 2.84 Å, Crystal structure of human Importin-beta (127-876) in complex with the IBB-domain of…
1M5N 2.9 Å, Crystal structure of HEAT repeats (1-11) of importin b bound to the non-classical…
2Q5D 3.2 Å, Crystal Structure of Human Importin Beta bound to the Snurportin1 IBB-domain second…

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