4WVF: KPT276

Crystal structure of KPT276 in complex with CRM1-Ran-RanBP1. Determined by X-ray diffraction at 1.8 Å resolution. Released 15 Jul 2015.

Method
X-ray diffraction
Resolution
1.8 Å
Organisms
Homo sapiens, Saccharomyces cerevisiae
Chains
3
Atoms
12,622
Mol. weight
159.82 kDa
Ligands
MG, K76, GNP
Released
15 Jul 2015

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

Secondary structure: helices and β-sheets

4WVF contains 86 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: 14 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-helix182-1865
α-helix188-1903
α-helix191-1933
α-helix194-20512
α-helix208-2092
Chain B: 2 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix66-683
β-strand83-97152
β-strand102-116152
β-strand122-12762
β-strand134-13962
β-strand14712
β-strand155-16392
β-strand170-17892
α-helix181-19919
Chain C: 70 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix0-56
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-helix137-14711
α-helix149-16315
α-helix164-1685
α-helix176-20227
α-helix208-22013
α-helix227-2304
α-helix234-2396
α-helix241-2444
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-helix544-56017
α-helix563-5686
α-helix570-58314
α-helix589-60618
α-helix608-6114
α-helix613-6142
α-helix621-6277
α-helix629-6324
α-helix638-65215
α-helix658-66811
α-helix670-68516
α-helix688-6914
α-helix693-71321
α-helix714-7174
α-helix718-74629
α-helix748-7525
α-helix754-77623
α-helix780-7823
α-helix783-7886
α-helix789-80113
α-helix804-8063
α-helix809-82214
α-helix823-8253
α-helix827-84519
α-helix853-86917
α-helix872-8754
α-helix879-89315
α-helix898-91821
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 1Bprotein140Saccharomyces cerevisiaeP41920 (AlphaFold model)
Crm1pCprotein1024Saccharomyces cerevisiaeP30822 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4WVF_1 GTP-binding nuclear protein Ran (chains A)
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIK
FNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC
GNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP
ALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
Sequence of entity 2 (B), FASTA
>4WVF_2 Ran-specific GTPase-activating protein 1 (chains B)
DIHFEPVVHLEKVDVKTMEEDEEVLYKVRAKLFRFDADAKEWKERGTGDCKFLKNKKTNK
VRILMRRDKTLKICANHIIAPEYTLKPNVGSDRSWVYACTADIAEGEAEAFTFAIRFGSK
ENADKFKEEFEKAQEINKKA
Sequence of entity 3 (C), FASTA
>4WVF_3 Crm1p (chains C)
GGSMEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEILTKFQDNPDAWQKADQILQF
STNPQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINK
SDLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQA
KALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILEL
LSTKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADL
KATYANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEERE
LFKTTLDYWHNLVADLFYEPLKKHIYEEICSQLRLVIIENMVRPEEVLVVENDEGEIVRE
FVKESDTIQLYKSEREVLVYLTHLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGS
ISGTMSEDTEKRFVVTVIKDLLDLCVKKRGKDNKAVVASDIMYVVGQYPRFLKAHWNFLR
TVILKLFEFMHETHEGVQDMACDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTA
DLQPQQVHTFYKACGIIISEERSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSE
TVKIIANIIKTNVAVCTSMGADFYPQLGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTP
KVRGLRTIKKEILKLVETYISKARNLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNC
MTTVVEKVGHMIPQGVILILQSVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAF
LELPPAAFKLFVDAICWAFKHNNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFI
FVSETFFVLTDSDHKSGFSKQALLLMKLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQY
LANMLSNAFPHLTSEQIASFLSALTKQCKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAED
KENA

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1
K76(2E)-3-{3-[3,5-bis(trifluoromethyl)phenyl]-1H-1,2,4-triazol-1-yl}-1-(3,3-difluo…C16 H10 F8 N4 O1
GNPPhosphoaminophosphonic acid-guanylate esterC10 H17 N6 O13 P31

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

Primary citation

Nuclear export inhibitors avert progression in preclinical models of inflammatory demyelination. Haines, J.D., Herbin, O., de la Hera, B. et al. Nat Neurosci (2015) 18:511-520. DOI 10.1038/nn.3953 · 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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