4GMX: KPT185

Crystal structure of KPT185 in complex with CRM1-Ran-RanBP1. Determined by X-ray diffraction at 2.1 Å resolution. Released 17 Oct 2012.

Method
X-ray diffraction
Resolution
2.1 Å
Organisms
Homo sapiens, Saccharomyces cerevisiae
Chains
3
Atoms
12,477
Mol. weight
163.91 kDa
Ligands
K85, MG, GNP
Released
17 Oct 2012

Explore 4GMX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4GMX contains 83 α-helices and 16 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: 12 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand10-1781
α-helix23-3210
β-strand45-55111
β-strand57-66101
α-helix70-723
α-helix76-805
β-strand85-9171
α-helix95-995
α-helix101-11111
β-strand117-12261
α-helix133-1353
α-helix138-1425
β-strand145-14841
α-helix159-16911
β-strand17611
α-helix178-1803
α-helix182-1854
α-helix200-2056
α-helix208-2092
Chain B: 1 helix, 7 β-strands
ElementResiduesLengthSheet
β-strand83-97152
β-strand102-116152
β-strand122-12872
β-strand134-13962
β-strand14712
β-strand155-16392
β-strand170-17782
α-helix181-19919
Chain C: 70 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix0-56
α-helix10-112
α-helix13-2513
α-helix28-4316
α-helix47-504
α-helix51-577
α-helix61-7818
α-helix79-813
α-helix84-10320
α-helix105-1106
α-helix112-12918
α-helix137-14610
α-helix149-16315
α-helix164-1685
α-helix176-20227
α-helix208-22013
α-helix227-2304
α-helix234-2363
α-helix237-2415
α-helix242-2443
α-helix246-25914
α-helix269-28517
α-helix286-2905
α-helix297-3037
α-helix308-32619
α-helix328-3314
α-helix334-3363
α-helix337-35014
α-helix356-37520
α-helix417-4204
α-helix421-43313
α-helix435-4384
β-strand443-44533
β-strand451-45333
α-helix459-4613
α-helix462-47817
α-helix480-49516
α-helix502-51413
α-helix521-54121
α-helix545-56117
α-helix563-5686
α-helix570-58314
α-helix589-60618
α-helix608-6114
α-helix621-6277
α-helix629-6324
α-helix638-65215
α-helix658-66811
α-helix670-68516
α-helix693-71321
α-helix714-7174
α-helix718-74629
α-helix748-7525
α-helix754-77623
α-helix780-7823
α-helix783-7886
α-helix789-80012
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-helix987-100216
α-helix1008-102013
α-helix1025-103814
α-helix1046-10505

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
GTP-binding nuclear protein RanAprotein216Homo sapiensP62826 (AlphaFold model)
Ran-specific GTPase-activating protein 1Bprotein141Saccharomyces cerevisiaeP41920 (AlphaFold model)
Exportin-1Cprotein1060Saccharomyces cerevisiaeP30822 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4GMX_1 GTP-binding nuclear protein Ran (chains A)
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIK
FNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC
GNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP
ALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
Sequence of entity 2 (B), FASTA
>4GMX_2 Ran-specific GTPase-activating protein 1 (chains B)
SDIHFEPVVHLEKVDVKTMEEDEEVLYKVRAKLFRFDADAKEWKERGTGDCKFLKNKKTN
KVRILMRRDKTLKICANHIIAPEYTLKPNVGSDRSWVYACTADIAEGEAEAFTFAIRFGS
KENADKFKEEFEKAQEINKKA
Sequence of entity 3 (C), FASTA
>4GMX_3 Exportin-1 (chains C)
GAMEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEILTKFQDNPDAWQKADQILQFS
TNPQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINKS
DLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQAK
ALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILELL
STKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADLK
ATYANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEEREL
FKTTLDYWHNLVADLFYEVQRLPATEMSPLIQLSVGSQAISTGSGALNPEYMKRFPLKKH
IYEEICSQLRLVIIENMVRPEEVLVVENDEGEIVREFVKESDTIQLYKSEREVLVYLTHL
NVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGSISGTMSEDTEKRFVVTVIKDLLDL
CVKKRGKDNKAVVASDIMYVVGQYPRFLKAHWNFLRTVILKLFEFMHETHEGVQDMACDT
FIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTADLQPQQVHTFYKACGIIISEERSV
AERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSETVKIIANIIKTNVAVCTSMGADFY
PQLGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTPKVRGLRTIKKEILKLVETYISKAR
NLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNCMTTVVEKVGHMIPQGVILILQSVF
ECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAFLELPPAAFKLFVDAICWAFKHNNR
DVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFIFVSETFFVLTDSDHKSGFSKQALL
LMKLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQYLANMLSNAFPHLTSEQIASFLSAL
TKQCKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAEDKENA

Ligands and cofactors

IDNameFormulaCopies
K85propan-2-yl 3-{3-[3-methoxy-5-(trifluoromethyl)phenyl]-1H-1,2,4-triazol-1-yl}pr…C16 H18 F3 N3 O31
MGMagnesium ionMg1
GNPPhosphoaminophosphonic acid-guanylate esterC10 H17 N6 O13 P31

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

Primary citation

Selective inhibitors of nuclear export show that CRM1/XPO1 is a target in chronic lymphocytic leukemia. Lapalombella, R., Sun, Q., Williams, K. et al. Blood (2012) 120:4621-4634. DOI 10.1182/blood-2012-05-429506 · 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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