3NC1: CRM1-RanGTP complex

Crystal structure of the CRM1-RanGTP complex. Determined by X-ray diffraction at 3.35 Å resolution. Released 27 Oct 2010.

Method: X-ray diffraction
Resolution: 3.35 Å
Organisms: Homo sapiens, Mus musculus
Chains: 2
Atoms: 9,749
Mol. weight: 144.65 kDa
Ligands: GTP, MG
Released: 27 Oct 2010

Explore 3NC1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3NC1 contains 77 α-helices and 11 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: 69 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	24-31	8
α-helix	41-51	11
α-helix	60-62	3
α-helix	63-67	5
α-helix	73-90	18
α-helix	96-114	19
α-helix	124-140	17
α-helix	149-152	4
α-helix	161-175	15
α-helix	176-180	5
β-strand	183	1	2
β-strand	186	1	2
α-helix	188-198	11
α-helix	203-214	12
α-helix	219-230	12
α-helix	232-234	3
α-helix	239-242	4
α-helix	247-253	7
α-helix	261-271	11
α-helix	280-295	16
α-helix	304-309	6
α-helix	313-332	20
α-helix	334-339	6
α-helix	341-343	3
α-helix	344-356	13
α-helix	357-359	3
α-helix	363-383	21
α-helix	407-422	16
β-strand	430-434	5	3
β-strand	440-444	5	3
α-helix	450-463	14
α-helix	469-484	16
α-helix	491-501	11
α-helix	510-530	21
α-helix	534-549	16
α-helix	552-557	6
α-helix	559-572	14
α-helix	580-594	15
α-helix	596-600	5
α-helix	602-603	2
α-helix	610-616	7
α-helix	627-643	17
α-helix	647-655	9
α-helix	657-659	3
α-helix	660-673	14
α-helix	678-680	3
α-helix	682-702	21
α-helix	704-706	3
α-helix	707-735	29
α-helix	737-741	5
α-helix	743-764	22
α-helix	769-775	7
α-helix	777-780	4
α-helix	781-785	5
α-helix	786-790	5
α-helix	793-795	3
α-helix	799-811	13
α-helix	812-814	3
α-helix	816-818	3
α-helix	819-826	8
α-helix	828-834	7
α-helix	842-857	16
α-helix	861-864	4
α-helix	868-881	14
α-helix	887-904	18
α-helix	908-917	10
α-helix	919-930	12
α-helix	939-951	13
α-helix	971-985	15
α-helix	991-1003	13
α-helix	1008-1019	12
α-helix	1021-1023	3
α-helix	1035-1046	12

Chain C: 8 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	9-17	9	1
α-helix	23-31	9
β-strand	45-54	10	1
β-strand	57-66	10	1
α-helix	70-72	3
α-helix	76-78	3
β-strand	85-91	7	1
α-helix	95-99	5
α-helix	101-111	11
β-strand	117-122	6	1
α-helix	133-135	3
α-helix	138-141	4
β-strand	145-147	3	1
α-helix	159-169	11
β-strand	176	1	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
GTP-binding nuclear protein Ran	C	protein	182	Homo sapiens	P62826 (AlphaFold model)
Exportin-1	A	protein	1073	Mus musculus	Q6P5F9 (AlphaFold model)

Sequence of entity 1 (C), FASTA

>3NC1_1 GTP-binding nuclear protein Ran (chains C)
GSMAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGP
IKFNVWDTAGLEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIV
LCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVA
MP

Sequence of entity 2 (A), FASTA

>3NC1_2 Exportin-1 (chains A)
GSMPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPD
AWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPT
CVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEV
FDFSSGQITQVKAKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPL
GYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFETLFTLTMMQLKQML
PLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHGQLLEKRLNLREALMEALHYMLLVS
EVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDIPPRRQLYLTVLSKVRL
LMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTEIIMTK
KLQNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKA
IIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRH
FVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYM
LLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDML
NVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVP
PLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDF
EEYPEHRTNFFLLLQAVNSHCFPAFLAIPPAQFKLVLDSIIWAFKHTMRNVADTGLQILF
TLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKI
STPLNPGNPVNNQMFIQDYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDF
LVQIKEFAGEDTSDLFLEERETALRQAQEEKHKLQMSVPGILNPHEIPEEMCD

Ligands and cofactors

ID	Name	Formula	Copies
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	1
MG	Magnesium ion	Mg	1

Primary citation

NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1. Guttler, T., Madl, T., Neumann, P. et al. Nat Struct Mol Biol (2010) 17:1367-1376. DOI 10.1038/nsmb.1931 · PubMed

Other PDB entries of the same protein (UniProt P62826 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3GJ0 1.48 Å, Crystal structure of human RanGDP
7MO5 1.55 Å, Crystal Structure of the ZnF4 of Nucleoporin NUP153 in complex with Ran-GDP
7MO1 1.6 Å, Crystal Structure of the ZnF1 of Nucleoporin NUP153 in complex with Ran-GDP
5CIQ 1.65 Å, Ran GDP wild type tetragonal crystal form
7MO2 1.65 Å, Crystal Structure of the ZnF2 of Nucleoporin NUP153 in complex with Ran-GDP
5CIT 1.75 Å, Ran GDP wild type monoclinic crystal form
5CIW 1.75 Å, Ran GDP Y39A mutant monoclinic crystal form
5CJ2 1.75 Å, Ran GDP Y39A mutant triclinic crystal form
1I2M 1.76 Å, Ran-RCC1-SO4 complex
4HAT 1.78 Å, Crystal structure of CRM1 inhibitor Leptomycin B in complex with CRM1-Ran-RanBP1
3GJ3 1.79 Å, Crystal structure of human RanGDP-Nup153ZnF2 complex
3GJ5 1.79 Å, Crystal structure of human RanGDP-Nup153ZnF4 complex

Browse structure collections

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