2BKU: Kap95p:RanGTP complex

Kap95p:RanGTP complex. Determined by X-ray diffraction at 2.7 Å resolution. Released 4 May 2005.

Method: X-ray diffraction
Resolution: 2.7 Å
Organisms: CANIS FAMILIARIS, SACCHAROMYCES CEREVISIAE
Chains: 4
Atoms: 16,104
Mol. weight: 231.48 kDa
Ligands: MG, GTP
Released: 4 May 2005

Explore 2BKU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2BKU contains 132 α-helices and 16 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: 7 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	10-16	7	1
α-helix	23-32	10
β-strand	45-55	11	1
β-strand	57-66	10	1
α-helix	70-72	3
α-helix	76-80	5
β-strand	85-91	7	1
α-helix	95-99	5
α-helix	101-109	9
β-strand	117-122	6	1
α-helix	138-141	4
β-strand	145-148	4	1
β-strand	150	1	2
β-strand	155	1	2
α-helix	159-169	11

Chain B: 59 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-35	17
α-helix	37-49	13
α-helix	55-66	12
α-helix	74-87	14
α-helix	90-104	15
α-helix	109-126	18
α-helix	127-129	3
α-helix	135-142	8
α-helix	149-165	17
α-helix	177-188	12
α-helix	195-208	14
α-helix	213-216	4
α-helix	219-233	15
α-helix	238-255	18
α-helix	256-258	3
α-helix	260-262	3
α-helix	263-267	5
α-helix	268-276	9
α-helix	280-306	27
α-helix	317-332	16
α-helix	347-362	16
α-helix	363-366	4
α-helix	367-377	11
α-helix	383-395	13
α-helix	402-418	17
α-helix	419-421	3
α-helix	425-442	18
α-helix	443-445	3
α-helix	452-463	12
α-helix	467-485	19
α-helix	493-495	3
α-helix	496-507	12
α-helix	513-515	3
α-helix	516-529	14
α-helix	533-535	3
α-helix	537-554	18
α-helix	563-584	22
α-helix	588-590	3
α-helix	595-607	13
α-helix	612-629	18
α-helix	630-633	4
α-helix	634-649	16
α-helix	655-669	15
α-helix	672-674	3
α-helix	675-688	14
α-helix	698-713	16
α-helix	714-717	4
α-helix	718-730	13
α-helix	734-736	3
α-helix	741-764	24
α-helix	769-772	4
α-helix	773-775	3
α-helix	776-788	13
α-helix	790-793	4
α-helix	796-812	17
α-helix	819-821	3
α-helix	825-834	10
α-helix	842-859	18

Chain C: 7 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	10-16	7	3
α-helix	23-32	10
β-strand	45-54	10	3
β-strand	57-66	10	3
α-helix	70-72	3
α-helix	76-80	5
β-strand	85-91	7	3
α-helix	95-99	5
α-helix	101-109	9
β-strand	117-122	6	3
α-helix	138-141	4
β-strand	145-148	4	3
β-strand	150	1	4
β-strand	155	1	4
α-helix	159-169	11

Chain D: 59 helices, 0 β-strands

Element	Residues	Length
α-helix	3-15	13
α-helix	19-35	17
α-helix	37-48	12
α-helix	55-66	12
α-helix	74-87	14
α-helix	90-104	15
α-helix	109-126	18
α-helix	127-129	3
α-helix	135-142	8
α-helix	149-165	17
α-helix	171-175	5
α-helix	177-188	12
α-helix	195-207	13
α-helix	213-216	4
α-helix	219-232	14
α-helix	238-254	17
α-helix	256-258	3
α-helix	260-262	3
α-helix	263-267	5
α-helix	268-275	8
α-helix	280-306	27
α-helix	317-320	4
α-helix	322-332	11
α-helix	347-362	16
α-helix	363-366	4
α-helix	367-377	11
α-helix	383-394	12
α-helix	402-418	17
α-helix	419-421	3
α-helix	425-441	17
α-helix	443-445	3
α-helix	452-463	12
α-helix	467-485	19
α-helix	493-495	3
α-helix	496-507	12
α-helix	513-515	3
α-helix	516-529	14
α-helix	533-535	3
α-helix	536-554	19
α-helix	565-584	20
α-helix	588-590	3
α-helix	595-607	13
α-helix	612-629	18
α-helix	630-633	4
α-helix	634-648	15
α-helix	655-669	15
α-helix	672-674	3
α-helix	675-689	15
α-helix	698-713	16
α-helix	714-720	7
α-helix	721-730	10
α-helix	741-764	24
α-helix	769-772	4
α-helix	773-775	3
α-helix	776-788	13
α-helix	790-793	4
α-helix	796-810	15
α-helix	825-834	10
α-helix	842-859	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
GTP-binding nuclear protein ran	A, C	protein	177	CANIS FAMILIARIS	P62825 (AlphaFold model)
Importin beta-1 subunit	B, D	protein	861	SACCHAROMYCES CEREVISIAE	Q06142 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>2BKU_1 GTP-BINDING NUCLEAR PROTEIN RAN (chains A, C)
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVPTLGVEVHPLVFHTNRGPIK
FNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC
GNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFV

Sequence of entity 2 (B, D), FASTA

>2BKU_2 IMPORTIN BETA-1 SUBUNIT (chains B, D)
MSTAEFAQLLENSILSPDQNIRLTSETQLKKLSNDNFLQFAGLSSQVLIDENTKLEGRIL
AALTLKNELVSKDSVKTQQFAQRWITQVSPEAKNQIKTNALTALVSIEPRIANAAAQLIA
AIADIELPHGAWPELMKIMVDNTGAEQPENVKRASLLALGYMCESADPQSQALVSSSNNI
LIAIVQGAQSTETSKAVRLAALNALADSLIFIKNNMEREGERNYLMQVVCEATQAEDIEV
QAAAFGCLCKIMSKYYTFMKPYMEQALYALTIATMKSPNDKVASMTVEFWSTICEEEIDI
AYELAQFPQSPLQSYNFALSSIKDVVPNLLNLLTRQNEDPEDDDWNVSMSAGACLQLFAQ
NCGNHILEPVLEFVEQNITADNWRNREAAVMAFGSIMDGPDKVQRTYYVHQALPSILNLM
NDQSLQVKETTAWCIGRIADSVAESIDPQQHLPGVVQACLIGLQDHPKVATNCSWTIINL
VEQLAEATPSPIYNFYPALVDGLIGAANRIDNEFNARASAFSALTTMVEYATDTVAETSA
SISTFVMDKLGQTMSVDENQLTLEDAQSLQELQSNILTVLAAVIRKSPSSVEPVADMLMG
LFFRLLEKKDSAFIEDDVFYAISALAASLGKGFEKYLETFSPYLLKALNQVDSPVSITAV
GFIADISNSLEEDFRRYSDAMMNVLAQMISNPNARRELKPAVLSVFGDIASNIGADFIPY
LNDIMALCVAAQNTKPENGTLEALDYQIKVLEAVLDAYVGIVAGLHDKPEALFPYVGTIF
QFIAQVAEDPQLYSEDATSRAAVGLIGDIAAMFPDGSIKQFYGQDWVIDYIKRTRSGQLF
SQATKDTARWAREQQKRQLSL

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	2

Primary citation

Structural Basis for Nuclear Import Complex Dissociation by Rangtp. Lee, S.J., Matsuura, Y., Liu, S.M. et al. Nature (2005) 435:693. DOI 10.1038/NATURE03578 · PubMed

Other PDB entries of the same protein (UniProt P62825 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1WA5 2.0 Å, Structure of the Cse1:Imp-alpha:RanGTP complex
1BYU 2.15 Å, Canine GDP-ran
3RAN 2.15 Å, Canine GDP-ran Q69L mutant
1QG2 2.5 Å, Canine GDP-ran R76E mutant
1QG4 2.5 Å, Canine GDP-ran F72Y mutant
5BXQ 2.5 Å, Structure of the NTF2:RanGDP complex
3W3Z 2.7 Å, Crystal structure of Kap121p bound to RanGTP
3A6P 2.92 Å, Crystal structure of Exportin-5:RanGTP:pre-miRNA complex
5YU6 3.0 Å, Crystal structure of exportin-5:RANGTP complex

Browse structure collections

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