5AZF: LGG-1

Crystal structure of LGG-1 complexed with a WEEL peptide. Determined by X-ray diffraction at 1.6 Å resolution. Released 30 Dec 2015.

Method: X-ray diffraction
Resolution: 1.6 Å
Organisms: Caenorhabditis elegans, Saccharomyces cerevisiae
Chains: 4
Atoms: 2,528
Mol. weight: 31.27 kDa
Ligands: CD
Released: 30 Dec 2015

Explore 5AZF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5AZF contains 14 α-helices and 18 β-strands across 4 chains. 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: 7 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	4-8	5
α-helix	11-24	14
β-strand	29-35	7	1
α-helix	36	1
α-helix	42-44	3
β-strand	48-51	4	1
β-strand	56	1	2
α-helix	57-67	11
β-strand	77-79	3	1
β-strand	80	1	3
β-strand	83	1	3
α-helix	84-86	3
β-strand	90	1	2
α-helix	91-98	8
β-strand	105-110	6	1

Chain B: 7 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	4-8	5
α-helix	11-24	14
β-strand	28-35	8	4
α-helix	36	1
α-helix	42-44	3
β-strand	48-52	5	4
β-strand	56	1	5
α-helix	57-67	11
β-strand	77-79	3	4
β-strand	80	1	6
β-strand	83	1	6
α-helix	84-86	3
β-strand	90	1	5
α-helix	91-98	8
β-strand	105-110	6	4

Chains C and D: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	2-3	2	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein lgg-1	A, B	protein	119	Caenorhabditis elegans	Q09490 (AlphaFold model)
peptide from Autophagy-related protein 19	C, D	protein	4	Saccharomyces cerevisiae	P35193 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5AZF_1 Protein lgg-1 (chains A, B)
GPHMKWAYKEENNFEKRRAEGDKIRRKYPDRIPVIVEKAPKSKLHDLDKKKYLVPSDLTV
GQFYFLIRKRIQLRPEDALFFFVNNVIPQTMTTMGQLYQDHHEEDLFLYIAYSDESVYG

Sequence of entity 2 (C, D), FASTA

>5AZF_2 peptide from Autophagy-related protein 19 (chains C, D)
WEEL

Ligands and cofactors

ID	Name	Formula	Copies
CD	Cadmium ion	Cd	13

Water and common crystallization additives (SO4) are not listed.

Primary citation

Structural Basis of the Differential Function of the Two C. elegans Atg8 Homologs, LGG-1 and LGG-2, in Autophagy. Wu, F., Watanabe, Y., Guo, X.Y. et al. Mol Cell (2015) 60:914-929. DOI 10.1016/j.molcel.2015.11.019 · PubMed

Other PDB entries of the same protein (UniProt Q09490 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8TGF 1.6 Å, Crystal structure of cEPG5 LIR/LGG-1 complex
5AZG 1.81 Å, Crystal structure of LGG-1 complexed with a UNC-51 peptide
8TGX 2.62 Å, Crystal structure of C. elegans LGG-1

Browse structure collections

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