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Structure of human TRIP13, apo form

Analyse Structure of human TRIP13, apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VQ9
Type: protein
Length: 367 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pachytene checkpoint protein 2 homolog
UniProt: Q15645
Pockets: 5 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
D	Pachytene checkpoint protein 2 homolog	protein	367	46% helix, 17% strand	Q15645

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	115	0.48	0.79	20	empty
2	100	0.48	0.81	19	empty
3	122	0.48	0.79	22	empty
4	111	0.45	0.78	19	empty
5	154	0.41	0.74	24	empty

Compared structures

5VQ9 · Structure of human TRIP13, Apo form · the same entry in another collection · chain D against D, TM-score 1.00
Q15645 · AlphaFold monomer V2.0 prediction for pachytene checkpoint protein 2 homolog (Q15645) · a predicted model of the same protein · chain D against A, TM-score 0.98

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q15645
Elsewhere: RCSB PDB 5VQ9 · PDBe 5VQ9 · UniProt Q15645

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