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Crystal structure of fission yeast ATG8 complexed with the helical aim of HFL1.

Analyse Crystal structure of fission yeast ATG8 complexed with the helical aim of HFL1. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6AAF
Type: protein
Length: 134 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Autophagy-related protein 8; Transmembrane protein 184 homolog C30D11.06C
UniProt: O94272, Q09906

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Autophagy-related protein 8	protein	112	35% helix, 23% strand	O94272
B	Transmembrane protein 184 homolog C30D11.06C	protein	22	41% helix, 0% strand	Q09906

Interfaces

1 interface between chains.

A–B · 1052 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

6AAF · Crystal structure of fission yeast Atg8 complexed with the helical AIM of Hfl1. · the same entry in another collection · chain A against A, TM-score 1.00
O94272 · AlphaFold monomer V2.0 prediction for autophagy-related protein 8 (O94272) · a predicted model of the same protein · chain A against A, TM-score 0.98
Q09906 · AlphaFold monomer V2.0 prediction for transmembrane protein 184 homolog C30D11.06C… · a predicted model of the same protein · chain B against A, TM-score 0.53

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 O94272
Every structure of UniProt Q09906
Elsewhere: RCSB PDB 6AAF · PDBe 6AAF · UniProt O94272 · UniProt Q09906

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