Crystal structure of human CRM1 covalently modified by 2-mercaptoethanol at Cys528. Determined by X-ray diffraction at 2.58 Å resolution. Released 10 Mar 2021.
Explore 7B51 in 3D Show helices and sheets RCSB PDB PDBe
7B51 contains 79 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-13 | 4 | |
| α-helix | 14-17 | 4 | |
| α-helix | 22-23 | 2 | |
| α-helix | 25-37 | 13 | |
| α-helix | 40-55 | 16 | |
| α-helix | 59-62 | 4 | |
| α-helix | 63-69 | 7 | |
| α-helix | 73-90 | 18 | |
| α-helix | 91-93 | 3 | |
| α-helix | 96-115 | 20 | |
| α-helix | 117-122 | 6 | |
| α-helix | 124-145 | 22 | |
| α-helix | 149-159 | 11 | |
| α-helix | 161-179 | 19 | |
| α-helix | 188-200 | 13 | |
| α-helix | 202-215 | 14 | |
| 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 | 313-338 | 26 | |
| α-helix | 341-343 | 3 | |
| α-helix | 344-357 | 14 | |
| α-helix | 363-383 | 21 | |
| α-helix | 404-409 | 6 | |
| α-helix | 413-423 | 11 | |
| α-helix | 424-426 | 3 | |
| β-strand | 430-434 | 5 | 4 |
| β-strand | 440-444 | 5 | 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 | 580-595 | 16 | |
| α-helix | 596-599 | 4 | |
| α-helix | 602-603 | 2 | |
| α-helix | 610-615 | 6 | |
| α-helix | 618-621 | 4 | |
| α-helix | 627-642 | 16 | |
| 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 | 743-765 | 23 | |
| α-helix | 769-775 | 7 | |
| α-helix | 780 | 1 | |
| α-helix | 781-785 | 5 | |
| α-helix | 786-790 | 5 | |
| α-helix | 793-795 | 3 | |
| α-helix | 799-811 | 13 | |
| α-helix | 813-816 | 4 | |
| α-helix | 819-831 | 13 | |
| α-helix | 842-858 | 17 | |
| α-helix | 861-865 | 5 | |
| α-helix | 868-881 | 14 | |
| α-helix | 887-904 | 18 | |
| α-helix | 908-930 | 23 | |
| α-helix | 933-938 | 6 | |
| α-helix | 939-955 | 17 | |
| α-helix | 970-985 | 16 | |
| α-helix | 991-1003 | 13 | |
| α-helix | 1008-1021 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-17 | 9 | 1 |
| α-helix | 23-32 | 10 | |
| α-helix | 41-43 | 3 | |
| β-strand | 45-52 | 8 | 1 |
| β-strand | 53-54 | 2 | 2 |
| β-strand | 59-66 | 8 | 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 | 133-135 | 3 | |
| α-helix | 138-141 | 4 | |
| β-strand | 145-148 | 4 | 1 |
| β-strand | 150 | 1 | 3 |
| β-strand | 155 | 1 | 3 |
| α-helix | 159-169 | 11 | |
| β-strand | 176-177 | 2 | 2 |
| 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) |
>7B51_1 GTP-binding nuclear protein Ran (chains B) MGMAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGP IKFNVWDTAGLEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIV LCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVA MP
>7B51_2 Exportin-1 (chains A) MASMTGGQQMGRGSMPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMA QEVLTHLKEHPDAWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYV VGLIIKTSSDPTCVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQN NMVILKLLSEEVFDFSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATL ETLLRFLNWIPLGYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTL FTLTMMQLKQMLPLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRET LMEALHYMLLVSEVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRR QLYLPMLFKVRLLMVSRMAKPEEAAAVENDQGEVVREFMKDTDSINLYKNMRETLVYLTH LDYVDTERIMTEKLHNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLG LCEQKRGKDNKAIIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACD TFIKIAQKCRRHFVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTD QTVQEHLIEKYMLLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPF VIQLGRIYLDMLNVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRS NDPQMVAENFVPPLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAV FECTLNMINKDFEEYPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTM RNVADTGLQILFTLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASIL AYMFNLVEEGKISTSLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQ DIPAFKEHLRDFLVQIKEFAGEDTSDLFLERSRSHHHHHH
Water and common crystallization additives (BME) are not listed.
Crystal structure of human CRM1, covalently modified by 2-mercaptoethanol on Cys528, in complex with RanGTP. Shaikhqasem, A., Schmitt, K., Valerius, O. et al. Acta Crystallogr F Struct Biol Commun (2021) 77:70-78. DOI 10.1107/S2053230X2100203X · PubMed
Other PDB entries of the same protein (UniProt P62826 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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