3GB8: CRM1/Snurportin-1 complex

Crystal structure of CRM1/Snurportin-1 complex. Determined by X-ray diffraction at 2.9 Å resolution. Released 31 Mar 2009.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Homo sapiens
Chains: 2
Atoms: 9,750
Mol. weight: 161.29 kDa
Released: 31 Mar 2009

Explore 3GB8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3GB8 contains 72 α-helices and 12 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: 60 helices, 0 β-strands

Element	Residues	Length
α-helix	63-68	6
α-helix	76-89	14
α-helix	97-113	17
α-helix	124-141	18
α-helix	149-157	9
α-helix	161-175	15
α-helix	188-197	10
α-helix	199-215	17
α-helix	219-232	14
α-helix	238-242	5
α-helix	246-249	4
α-helix	250-255	6
α-helix	258-260	3
α-helix	261-273	13
α-helix	280-297	18
α-helix	304-310	7
α-helix	313-339	27
α-helix	341-343	3
α-helix	344-358	15
α-helix	363-383	21
α-helix	404-423	20
α-helix	424-427	4
α-helix	448-467	20
α-helix	469-484	16
α-helix	491-503	13
α-helix	510-530	21
α-helix	534-550	17
α-helix	552-557	6
α-helix	559-572	14
α-helix	580-595	16
α-helix	596-598	3
α-helix	610-615	6
α-helix	618-622	5
α-helix	627-642	16
α-helix	647-674	28
α-helix	676-680	5
α-helix	682-702	21
α-helix	704-706	3
α-helix	707-732	26
α-helix	737-740	4
α-helix	743-765	23
α-helix	769-771	3
α-helix	772-776	5
α-helix	777-790	14
α-helix	793-795	3
α-helix	798-811	14
α-helix	812-814	3
α-helix	816-818	3
α-helix	819-835	17
α-helix	842-858	17
α-helix	862-865	4
α-helix	868-883	16
α-helix	887-904	18
α-helix	908-931	24
α-helix	939-954	16
α-helix	970-985	16
α-helix	991-1002	12
α-helix	1008-1023	16
α-helix	1031-1052	22
α-helix	1053-1055	3

Chain B: 12 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	1-10	10
α-helix	26-28	3
α-helix	32-33	2
α-helix	41-52	12
α-helix	59-64	6
β-strand	103-107	5	1
α-helix	115-118	4
β-strand	119-125	7	1
β-strand	128-135	8	2
β-strand	138-142	5	2
β-strand	148-152	5	2
β-strand	170-177	8	2
β-strand	182-191	10	2
β-strand	194-195	2	2
α-helix	201-211	11
β-strand	228-231	4	2
α-helix	232-233	2
β-strand	234-236	3	1
α-helix	239-247	9
β-strand	254-261	8	1
α-helix	264-266	3
β-strand	269-277	9	1
α-helix	279-281	3
α-helix	282-286	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Exportin-1	A	protein	1071	Homo sapiens	O14980 (AlphaFold model)
Snurportin-1	B	protein	329	Homo sapiens	O95149 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3GB8_1 Exportin-1 (chains A)
MPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPDAW
TRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPTCV
EKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEVFD
FSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPLGY
IFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTLFTLTMMQLKQMLPL
NTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRETLMEALHYMLLVSEV
EETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRRQLYLPMLFKVRLLM
VSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTERIMTEKL
HNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKAII
ASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRHFV
QVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYMLL
PNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDMLNV
YKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVPPL
LDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDFEE
YPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTMRNVADTGLQILFTL
LQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKIST
SLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDFLV
QIKEFAGEDTSDLFLEEREIALRQADEEKHKRQMSVPGIFNPHEIPEEMCD

Sequence of entity 2 (B), FASTA

>3GB8_2 Snurportin-1 (chains B)
SMEELSQALASSFSVSQDLNSTAAPHPRLSQYKSKYSSLEQSERRRRLLELQKSKRLDYV
NHARRLAEDDWTGMESEEENKKDDEEMDIDTVKKLPKHYANQLMLSEWLIDVPSDLGQEW
IVVVCPVGKRALIVASRGSTSAYTKSGYCVNRFSSLLPGGNRRNSTAKDYTILDCIYNEV
NQTYYVLDVMCWRGHPFYDCQTDFRFYWMHSKLPEEEGLGEKTKLNPFKFVGLKNFPCTP
ESLCDVLSMDFPFEVDGLLFYHKQTHYSPGSTPLVGWLRPYMVSDVLGVAVPAGPLTTKP
DYAGHQLQQIMEHKKSQKEGMKEKLTHKA

Primary citation

Structural basis for leucine-rich nuclear export signal recognition by CRM1. Dong, X., Biswas, A., Suel, K.E. et al. Nature (2009) 458:1136-1141. DOI 10.1038/nature07975 · PubMed

Other PDB entries of the same protein (UniProt O14980 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1W9C 2.3 Å, Proteolytic fragment of CRM1 spanning six C-terminal HEAT repeats
9OGD 2.49 Å, Cryo-EM structure of human exportin-1 conjugated with selinexor and bound to human…
7B51 2.58 Å, Crystal structure of human CRM1 covalently modified by 2-mercaptoethanol at Cys528
9HFL 2.62 Å, Cryo-EM structure of the human snRNA export complex comprising CBC-PHAX-CRM1-RanGTP and…
5DIS 2.85 Å, Crystal structure of a CRM1-RanGTP-SPN1 export complex bound to a 113 amino acid…
9B62 2.9 Å, Human RANBP2/RAN(GTP)/RANGAP1-SUMO1/UBC9/CRM1/RAN(GTP) - composite map and model
9OG9 2.93 Å, Cryo-EM structure of human full-length XPO1 (unliganded)
11RM 2.95 Å, Cryo-EM structure of human exportin-1 conjugated with FR-027*
6TVO 3.2 Å, Human CRM1-RanGTP in complex with Leptomycin B
9OGB 3.25 Å, Cryo-EM structure of human exportin-1 conjugated with selinexor and bound to yeast…
9OGE 3.28 Å, Cryo-EM structure of human exportin-1 conjugated with KPT-127 and bound to human…
9OGA 3.37 Å, Cryo-EM structure of human full-length XPO1 conjugated with selinexor

Browse structure collections

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