5UWU: SMAD4 NES Peptide

Crystal Structure of SMAD4 NES Peptide in complex with CRM1-Ran-RanBP1. Determined by X-ray diffraction at 2.24 Å resolution. Released 22 Mar 2017.

Method
X-ray diffraction
Resolution
2.24 Å
Organisms
Homo sapiens, Saccharomyces cerevisiae
Chains
4
Atoms
11,641
Mol. weight
163.65 kDa
Ligands
GNP, MG
Released
22 Mar 2017

Explore 5UWU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5UWU contains 87 α-helices and 14 β-strands across 4 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-helix182-1876
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-strand147-14932
β-strand152-163122
β-strand170-17782
α-helix181-19919
Chain C: 72 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix1-55
α-helix10-112
α-helix13-2513
α-helix28-4215
α-helix47-504
α-helix51-577
α-helix61-7818
α-helix79-813
α-helix84-10320
α-helix105-1106
α-helix112-12918
α-helix137-1459
α-helix149-16315
α-helix164-1685
α-helix176-18813
α-helix190-20314
α-helix207-22014
α-helix227-2304
α-helix234-2396
α-helix241-2444
α-helix246-25914
α-helix269-28921
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-helix435-4373
α-helix462-47817
α-helix480-49516
α-helix502-51413
α-helix521-54121
α-helix545-56016
α-helix563-5686
α-helix570-58314
α-helix591-60616
α-helix608-6114
α-helix613-6142
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-helix783-7886
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-helix922-9276
α-helix928-9325
α-helix933-94412
α-helix949-9513
α-helix952-96716
α-helix987-100216
α-helix1008-102013
α-helix1025-103814
α-helix1046-10505
Chain D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix143-1453

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
GTP-binding nuclear protein RanAprotein237Homo sapiensP62826 (AlphaFold model)
Ran-specific GTPase-activating protein 1Bprotein143Saccharomyces cerevisiaeP41920 (AlphaFold model)
Exportin-1Cprotein1024Saccharomyces cerevisiaeP30822 (AlphaFold model)
Mothers against decapentaplegic homolog 4Dprotein20Homo sapiensQ13485 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5UWU_1 GTP-binding nuclear protein Ran (chains A)
METGSSHHHHHHSSGLPRGSHMAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKY
VATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYK
NVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEK
PFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
Sequence of entity 2 (B), FASTA
>5UWU_2 Ran-specific GTPase-activating protein 1 (chains B)
GGSDIHFEPVVHLEKVDVKTMEEDEEVLYKVRAKLFRFDADAKEWKERGTGDCKFLKNKK
TNKVRILMRRDKTLKICANHIIAPEYTLKPNVGSDRSWVYACTADIAEGEAEAFTFAIRF
GSKENADKFKEEFEKAQEINKKA
Sequence of entity 3 (C), FASTA
>5UWU_3 Exportin-1 (chains C)
GGSMEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEILTKFQDNPDAWQKADQILQF
STNPQSKFIALSILDKLITRKWKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINK
SDLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIVLKLLSEEVFDFSAEQMTQA
KALHLKNSMSKEFEQIFKLCFQVLEQGSSSSLIVATLESLLRYLHWIPYRYIYETNILEL
LSTKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFFQNTLQQIATSVMPVTADL
KATYANANGNDQSFLQDLAMFLTTYLARNRALLESDESLRELLLNAHQYLIQLSKIEERE
LFKTTLDYWHNLVADLFYEPLKKHIYEEICSQLRLVIIENMVRPEEDLVVENDEGEIVRE
FVKESDTIQLYKSEREVLVYLTHLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGS
ISGTMSEDTEKRFVVTVIKDLLGLCEQKRGKDNKAVVASDIMYVVGQYPRFLKAHWNFLR
TVILKLFEFMHETHEGVQDMACDTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTA
DLQPQQVHTFYKACGIIISEERSVAERNRLLSDLMQLPNMAWDTIVEQSTANPTLLLDSE
TVKIIANIIKTNVAVCTSMGADFYPQLGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTP
KVRGLRTIKKEILKLVETYISKARNLDDVVKVLVEPLLNAVLEDYMNNVPDARDAEVLNC
MTTVVEKVGHMIPQGVILILQSVFECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAF
LELPPAAFKLFVDAICWAFKHNNRDVEVNGLQIALDLVKNIERMGNVPFANEFHKNYFFI
FVSETFFVLTDSDHKSGFSKQALLLMKLISLVYDNKISVPLYQEAEVPQGTSNQVYLSQY
LANMLSNAFPHLTSEQIASFLSALTKQCKDLVVFKGTLRDFLVQIKEVGGDPTDYLFAED
KENA
Sequence of entity 4 (D), FASTA
>5UWU_4 Mothers against decapentaplegic homolog 4 (chains D)
GGSYERVVSPGIDLSGLTLQ

Ligands and cofactors

IDNameFormulaCopies
GNPPhosphoaminophosphonic acid-guanylate esterC10 H17 N6 O13 P31
MGMagnesium ionMg1

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

Primary citation

Nuclear export receptor CRM1 recognizes diverse conformations in nuclear export signals. Fung, H.Y., Fu, S.C., Chook, Y.M. Elife (2017) 6. DOI 10.7554/eLife.23961 · 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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