5VQ9: Human TRIP13, Apo form

Structure of human TRIP13, Apo form. Determined by X-ray diffraction at 3.02 Å resolution. Released 14 Jun 2017.

Method: X-ray diffraction
Resolution: 3.02 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,938
Mol. weight: 48.61 kDa
Released: 14 Jun 2017

Explore 5VQ9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5VQ9 contains 17 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 D: 17 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	20-27	8	1
α-helix	35-49	15
β-strand	57-58	2	1
α-helix	64-69	6
β-strand	70-76	7	1
β-strand	94-101	8	1
β-strand	103	1	2
β-strand	123-127	5	3
β-strand	129	1	2
α-helix	135-138	4
α-helix	145-162	18
β-strand	174-178	5	3
α-helix	185-199	15
β-strand	206-212	7	3
α-helix	213	1
α-helix	228-240	13
β-strand	245-251	7	3
α-helix	255-259	5
α-helix	273-287	15
β-strand	293-299	7	3
α-helix	309-312	4
β-strand	315-318	4	3
α-helix	321-323	3
α-helix	324-341	18
β-strand	344	1	4
α-helix	353-358	6
α-helix	368-379	12
α-helix	385-395	11
α-helix	396-400	5
β-strand	405	1	4
α-helix	407-429	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Pachytene checkpoint protein 2 homolog	D	protein	432	Homo sapiens	Q15645 (AlphaFold model)

Sequence of entity 1 (D), FASTA

>5VQ9_1 Pachytene checkpoint protein 2 homolog (chains D)
MDEAVGDLKQALPCVAESPTVHVEVHQRGSSTAKKEDINLSVRKLLNRHNIVFGDYTWTE
FDEPFLTRNVQSVSIIDTELKVKDSQPIDLSACTVALHIFQLNEDGPSSENLEEETENII
AANHWVLPAAEFHGLWDSLVYDVEVKSHLLDYVMTTLLFSDKNVNSNLITWNRVVLLHGP
PGTGKTSLCKALAQKLTIRLSSRYRYGQLIEINSHSLFSKWFSESGKLVTKMFQKIQDLI
DDKDALVFVLIDQVESLTAARNACRAGTEPSDAIRVVNAVLTQIDQIKRHSNVVILTTSN
ITEKIDVAFVDRADIKQYIGPPSAAAIFKIYLSCLEELMKCQIIYPRQQLLTLRELEMIG
FIENNVSKLSLLLNDISRKSEGLSGRVLRKLPFLAHALYVQAPTVTIEGFLQALSLAVDK
QFEERKKLAAYI

Primary citation

The AAA+ ATPase TRIP13 remodels HORMA domains through N-terminal engagement and unfolding. Ye, Q., Kim, D.H., Dereli, I. et al. EMBO J (2017) 36:2419-2434. DOI 10.15252/embj.201797291 · PubMed

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

5WC2 2.5 Å, Crystal Structure of ADP-bound human TRIP13
5VQA 2.54 Å, Structure of human TRIP13, ATP-bound form
6LK0 2.6 Å, Crystal structure of human wild type TRIP13
7L9P 3.6 Å, Structure of human SHLD2-SHLD3-REV7-TRIP13(E253Q) complex
6F0X 4.6 Å, Cryo-EM structure of TRIP13 in complex with ATP gamma S, p31comet, C-Mad2 and Cdc20

Browse structure collections

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