5WC2: ADP-bound human TRIP13

Crystal Structure of ADP-bound human TRIP13. Determined by X-ray diffraction at 2.5 Å resolution. Released 25 Apr 2018.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Homo sapiens
Chains
1
Atoms
3,060
Mol. weight
48.98 kDa
Ligands
ADP
Released
25 Apr 2018

Explore 5WC2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5WC2 contains 16 α-helices and 14 β-strands across 1 chain. 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: 16 helices, 14 β-strands

ElementResiduesLengthSheet
β-strand20-2781
α-helix35-4915
β-strand57-5821
α-helix64-696
β-strand70-7671
β-strand94-10181
β-strand10312
β-strand122-12763
β-strand12912
α-helix130-1323
α-helix135-1384
α-helix145-16117
β-strand174-17853
α-helix185-19915
β-strand206-21273
α-helix229-24012
β-strand245-25173
α-helix255-2595
α-helix273-28715
β-strand293-29973
α-helix308-3114
β-strand315-31843
α-helix321-3233
α-helix324-34017
β-strand34414
α-helix353-3586
α-helix368-37912
α-helix385-39915
β-strand40514
α-helix407-42822

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Pachytene checkpoint protein 2 homologAprotein432Homo sapiensQ15645 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5WC2_1 Pachytene checkpoint protein 2 homolog (chains A)
MDEAVGDLKQALPCVAESPTVHVEVHQRGSSTAKKEDINLSVRKLLNRHNIVFGDYTWTE
FDEPFLTRNVQSVSIIDTELKVKDSQPIDLSACTVALHIFQLNEDGPSSENLEEETENII
AANHWVLPAAEFHGLWDSLVYDVEVKSHLLDYVMTTLLFSDKNVNSNLITWNRVVLLHGP
PGTGKTSLCKALAQKLTIRLSSRYRYGQLIEINSHSLFSKWFSESGKLVTKMFQKIQDLI
DDKDALVFVLIDAVESLTAARNACRAGTEPSDAIRVVNAVLTQIDQIKRHSNVVILTTSN
ITEKIDVAFVDRADIKQYIGPPSAAAIFKIYLSCLEELMKCQIIYPRQQLLTLRELEMIG
FIENNVSKLSLLLNDISRKSEGLSGRVLRKLPFLAHALYVQAPTVTIEGFLQALSLAVDK
QFEERKKLAAYI

Ligands and cofactors

IDNameFormulaCopies
ADPAdenosine-5'-diphosphateC10 H15 N5 O10 P21

Primary citation

Mechanistic insight into TRIP13-catalyzed Mad2 structural transition and spindle checkpoint silencing. Brulotte, M.L., Jeong, B.C., Li, F. et al. Nat Commun (2017) 8:1956-1956. DOI 10.1038/s41467-017-02012-2 · PubMed

Other PDB entries of the same protein (UniProt Q15645 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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