6TVO: Human CRM1-RanGTP

Human CRM1-RanGTP in complex with Leptomycin B. Determined by X-ray diffraction at 3.2 Å resolution. Released 8 Jul 2020.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: Homo sapiens
Chains: 2
Atoms: 9,678
Mol. weight: 143.86 kDa
Ligands: GTP, MG, LMB
Released: 8 Jul 2020

Explore 6TVO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6TVO contains 77 α-helices and 13 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	10-15	6
α-helix	25-37	13
α-helix	41-55	15
α-helix	59-61	3
α-helix	63-69	7
α-helix	73-89	17
α-helix	91-93	3
α-helix	96-115	20
α-helix	117-119	3
α-helix	124-145	22
α-helix	149-159	11
α-helix	161-175	15
α-helix	176-180	5
β-strand	183	1	3
β-strand	186	1	3
α-helix	188-200	13
α-helix	202-215	14
α-helix	219-235	17
α-helix	239-242	4
α-helix	246-249	4
α-helix	250-254	5
α-helix	258-260	3
α-helix	261-273	13
α-helix	280-297	18
α-helix	304-310	7
α-helix	313-338	26
α-helix	341-343	3
α-helix	344-358	15
α-helix	363-383	21
α-helix	404-422	19
α-helix	424-426	3
β-strand	429-434	6	4
β-strand	440-445	6	4
α-helix	449-467	19
α-helix	469-484	16
α-helix	491-503	13
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	597-600	4
α-helix	602-603	2
α-helix	610-616	7
α-helix	618-621	4
α-helix	627-643	17
α-helix	647-657	11
α-helix	659-674	16
α-helix	676-680	5
α-helix	682-702	21
α-helix	704-706	3
α-helix	707-735	29
α-helix	738-741	4
α-helix	743-764	22
α-helix	769-771	3
α-helix	772-776	5
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	812-818	7
α-helix	819-831	13
α-helix	842-858	17
α-helix	860-864	5
α-helix	868-882	15
α-helix	887-906	20
α-helix	908-930	23
α-helix	936-938	3
α-helix	939-954	16
α-helix	970-985	16
α-helix	991-1003	13
α-helix	1008-1021	14

Chain B: 8 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	9-17	9	1
α-helix	23-32	10
α-helix	41-43	3
β-strand	45-55	11	1
β-strand	57-66	10	1
α-helix	78-80	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
β-strand	150	1	2
β-strand	155	1	2
α-helix	159-169	11
β-strand	176	1	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
GTP-binding nuclear protein Ran	B	protein	182	Homo sapiens	P62826 (AlphaFold model)
Exportin-1	A	protein	1060	Homo sapiens	O14980 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>6TVO_1 GTP-binding nuclear protein Ran (chains B)
MGMAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGP
IKFNVWDTAGLEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIV
LCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVA
MP

Sequence of entity 2 (A), FASTA

>6TVO_2 Exportin-1 (chains A)
MASMTGGQQMGRGSMPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMA
QEVLTHLKEHPDAWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYV
VGLIIKTSSDPTCVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQN
NMVILKLLSEEVFDFSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATL
ETLLRFLNWIPLGYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTL
FTLTMMQLKQMLPLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRET
LMEALHYMLLVSEVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRR
QLYLPMLFKVRLLMVSRMAKPEEAAAVENDQGEVVREFMKDTDSINLYKNMRETLVYLTH
LDYVDTERIMTEKLHNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLG
LCEQKRGKDNKAIIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACD
TFIKIAQKCRRHFVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTD
QTVQEHLIEKYMLLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPF
VIQLGRIYLDMLNVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRS
NDPQMVAENFVPPLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAV
FECTLNMINKDFEEYPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTM
RNVADTGLQILFTLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASIL
AYMFNLVEEGKISTSLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQ
DIPAFKEHLRDFLVQIKEFAGEDTSDLFLERSRSHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	1
MG	Magnesium ion	Mg	1
LMB	Leptomycin B, bound form	C33 H52 O7	1

Primary citation

Characterization of Inhibition Reveals Distinctive Properties for Human andSaccharomyces cerevisiaeCRM1. Shaikhqasem, A., Dickmanns, A., Neumann, P. et al. J Med Chem (2020) 63:7545-7558. DOI 10.1021/acs.jmedchem.0c00143 · 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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