6LK0: Human wild type TRIP13

Crystal structure of human wild type TRIP13. Determined by X-ray diffraction at 2.6 Å resolution. Released 22 Jan 2020.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,710
Mol. weight: 48.69 kDa
Released: 22 Jan 2020

Explore 6LK0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6LK0 contains 14 α-helices and 16 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: 14 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	22-27	6	1
α-helix	35-47	13
β-strand	57-58	2	1
α-helix	64-69	6
β-strand	70-75	6	1
β-strand	96-100	5	1
β-strand	103	1	2
β-strand	122-127	6	3
β-strand	129	1	2
α-helix	130-132	3
α-helix	135-138	4
α-helix	145-161	17
β-strand	174-178	5	3
α-helix	185-199	15
β-strand	206-212	7	3
α-helix	228-240	13
β-strand	245-252	8	3
α-helix	275-287	13
β-strand	293-299	7	3
β-strand	315-318	4	3
α-helix	321-323	3
α-helix	324-340	17
β-strand	344	1	4
α-helix	353-357	5
α-helix	368-378	11
β-strand	381	1	5
β-strand	383	1	5
α-helix	385-399	15
β-strand	405	1	4
α-helix	407-424	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Pachytene checkpoint protein 2 homolog	A	protein	433	Homo sapiens	Q15645 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6LK0_1 Pachytene checkpoint protein 2 homolog (chains A)
SMDEAVGDLKQALPCVAESPTVHVEVHQRGSSTAKKEDINLSVRKLLNRHNIVFGDYTWT
EFDEPFLTRNVQSVSIIDTELKVKDSQPIDLSACTVALHIFQLNEDGPSSENLEEETENI
IAANHWVLPAAEFHGLWDSLVYDVEVKSHLLDYVMTTLLFSDKNVNSNLITWNRVVLLHG
PPGTGKTSLCKALAQKLTIRLSSRYRYGQLIEINSHSLFSKWFSESGKLVTKMFQKIQDL
IDDKDALVFVLIDEVESLTAARNACRAGTEPSDAIRVVNAVLTQIDQIKRHSNVVILTTS
NITEKIDVAFVDRADIKQYIGPPSAAAIFKIYLSCLEELMKCQIIYPRQQLLTLRELEMI
GFIENNVSKLSLLLNDISRKSEGLSGRVLRKLPFLAHALYVQAPTVTIEGFLQALSLAVD
KQFEERKKLAAYI

Primary citation

A Small-Molecule Inhibitor Targeting TRIP13 Suppresses Multiple Myeloma Progression. Wang, Y., Huang, J., Li, B. et al. Cancer Res (2020) 80:536-548. DOI 10.1158/0008-5472.CAN-18-3987 · 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
5VQ9 3.02 Å, Structure of human TRIP13, Apo form
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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