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S. cerevisiae TY1 P22 restriction factor, gag ca-ctd, AUG2 variant

Analyse S. cerevisiae TY1 P22 restriction factor, gag ca-ctd, AUG2 variant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7NLI
Type: protein
Length: 274 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TY1 gag P22
UniProt: P08405
Pockets: 2 · best druggability 0.40

Structure

x-ray diffraction · 2 distinct chains · 63% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	TY1 gag P22	protein	91	64% helix, 3% strand	P08405
B	TY1 gag P22	protein	92	62% helix, 3% strand	P08405

Pockets

2 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	58	0.40	0.81	13	empty
2	54	0.38	0.80	13	empty

Interfaces

2 interfaces between chains.

A–B · 861 Å² buried · 9 hydrogen bonds · protein-protein
A–C · 741 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

7NLI · S. cerevisiae Ty1 p22 restriction factor, Gag CA-CTD, AUG2 variant · the same entry in another collection · chain A against A, TM-score 1.00
P08405 · AlphaFold monomer V2.0 prediction for transposon TYH3 gag polyprotein (P08405) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P08405
Elsewhere: RCSB PDB 7NLI · PDBe 7NLI · UniProt P08405

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