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Crystal structure of a hairpin exchange variant (ltx) of the targeting line-1 retrotransposon endonuclease

Analyse Crystal structure of a hairpin exchange variant (ltx) of the targeting line-1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2V0R
Type: protein
Length: 469 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ltx
UniProt: Q8TE30
Ligands: SO4
Pockets: 5 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ltx	protein	235	25% helix, 37% strand	Q8TE30
B	Ltx	protein	234	25% helix, 35% strand	Q8TE30

Ligands and binding sites

SO4 · Sulfate ion · ion · 6 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	532	0.68	0.78	57	empty
2	65	0.45	0.83	14	empty
3	76	0.43	0.80	11	empty
4	107	0.37	0.75	25	SO4
5	123	0.37	0.74	21	empty

Interfaces

1 interface between chains.

A–B · 1274 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

2V0R · crystal structure of a hairpin exchange variant (LTx) of the targeting LINE-1… · the same entry in another collection · chain A against A, TM-score 1.00

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 Q8TE30
Elsewhere: RCSB PDB 2V0R · PDBe 2V0R · UniProt Q8TE30

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