7DBG: Yeast CRM1e

Yeast CRM1e (apo) in complex with Ran-RanBP1. Determined by X-ray diffraction at 2.06 Å resolution. Released 29 Sept 2021.

Method
X-ray diffraction
Resolution
2.06 Å
Organisms
Homo sapiens, Saccharomyces cerevisiae
Chains
3
Atoms
11,398
Mol. weight
157.47 kDa
Ligands
MPO, GTP, MG
Released
29 Sept 2021

Explore 7DBG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7DBG contains 84 α-helices and 14 β-strands across 3 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: 14 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand9-1681
α-helix23-3210
β-strand45-54101
β-strand57-66101
α-helix70-723
α-helix76-794
β-strand85-9171
α-helix95-995
α-helix101-1099
β-strand117-12261
α-helix133-1353
α-helix138-1425
β-strand145-14841
α-helix159-16911
β-strand17611
α-helix178-1803
α-helix182-1865
α-helix191-1933
α-helix194-1974
α-helix201-2055
α-helix208-2092
Chain B: 1 helix, 7 β-strands
ElementResiduesLengthSheet
β-strand83-97152
β-strand102-116152
β-strand122-12762
β-strand134-13962
β-strand14712
β-strand155-16392
β-strand170-17782
α-helix181-19919
Chain C: 69 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix1-55
α-helix13-2513
α-helix28-4316
α-helix47-504
α-helix51-577
α-helix61-7717
α-helix79-813
α-helix84-10320
α-helix105-1106
α-helix112-12918
α-helix137-1459
α-helix149-16315
α-helix164-1685
α-helix170-1734
α-helix176-20328
α-helix207-22014
α-helix227-2304
α-helix234-2396
α-helix241-2444
α-helix246-26015
α-helix269-28921
α-helix297-3037
α-helix308-32619
α-helix327-3304
α-helix334-3363
α-helix337-35014
α-helix356-37520
α-helix417-4204
α-helix421-43313
α-helix435-4373
α-helix462-47817
α-helix480-49516
α-helix502-51413
α-helix521-54121
α-helix545-56117
α-helix563-5686
α-helix570-58314
α-helix591-60616
α-helix608-6114
α-helix621-6277
α-helix629-6335
α-helix638-65215
α-helix658-66811
α-helix670-68516
α-helix687-6915
α-helix693-71321
α-helix714-7174
α-helix718-74629
α-helix748-7525
α-helix754-77623
α-helix780-7823
α-helix783-7875
α-helix788-80013
α-helix804-8063
α-helix809-82214
α-helix823-8253
α-helix827-84519
α-helix853-86917
α-helix872-8754
α-helix879-89315
α-helix898-91720
α-helix922-94423
α-helix949-9513
α-helix952-96716
α-helix9771
α-helix987-100216
α-helix1008-102013
α-helix1025-103814
α-helix1046-10505

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
GTP-binding nuclear protein RanAprotein216Homo sapiensP62826 (AlphaFold model)
YRB1 isoform 1Bprotein140Saccharomyces cerevisiaeP41920 (AlphaFold model)
CRM1 isoform 1Cprotein1003Saccharomyces cerevisiaeP30822 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>7DBG_1 GTP-binding nuclear protein Ran (chains A)
MAAQGEPEVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIK
FNVWDTAGLEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC
GNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP
AAAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
Sequence of entity 2 (B), FASTA
>7DBG_2 YRB1 isoform 1 (chains B)
DIHFEPVVHLEKVDVKTMEEDEEVLYKVRAKLFRFDADAKEWKERGTGDCKFLKNKKTNK
VRILMRRDKTLKICANHIIAPEYTLKPNVGSDRSWVYACTADIAEGEAEAFTFAIRFGSK
ENADKFKEEFEKAQEINKKA
Sequence of entity 3 (C), FASTA
>7DBG_3 CRM1 isoform 1 (chains C)
GGSMEGILDFSNDLDIALLDQVVSTFYQGEGVQQKQAQEILTKFQDNPDAWEKVDQILQF
STNPQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINK
SDLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQA
KALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILEL
LSTKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADL
KATYANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEERE
LFKTTLDYWHNLVADLFYEPLKKHIYEEICSQLRLVIIENMVRPEEIQLYKSEREVLVYL
THLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGSISGTMSEDTEKRFVVTVIKDL
LGLCEQKRGKDNKAVVARDIMYVVGEYPRFLKAHWNFLRTVILKLFEFMHETHEGVQDMA
CDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTADLQPQQVHTFYKACGIIISEE
RSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSETVKIIANIIKTNVAVCTSMGA
DFYPQLGHIYYNMLQLYRAVSSMISTQVAAEGLIATKTPKVRGLRTIKKEILKLVETYIS
KARNLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNCMTTVVEKVGHMIPQGVILILQ
SVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAFLELPPAAFKLFVDAICWAFKH
NNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFIFVSETFFVLTDSDHKSGFSKQ
ALLLMKLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQYLANMLSNAFPHLTSEQIASFL
SALTKQCKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAEDKENA

Ligands and cofactors

IDNameFormulaCopies
MPO3[N-morpholino]propane sulfonic acidC7 H15 N O4 S1
GTPGuanosine-5'-triphosphateC10 H16 N5 O14 P31
MGMagnesium ionMg1

Water and common crystallization additives (DMS, CL, GOL) are not listed.

Primary citation

Novel Mechanistic Observations and NES-Binding Groove Features Revealed by the CRM1 Inhibitors Plumbagin and Oridonin. Lei, Y., Li, Y., Tan, Y. et al. J Nat Prod (2021) 84:1478-1488. DOI 10.1021/acs.jnatprod.0c01231 · PubMed

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

Browse structure collections

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