Research workbench

Structure of human ATG5 E122D-ATG16L1 complex at 3.0 ångströms

Analyse Structure of human ATG5 E122D-ATG16L1 complex at 3.0 ångströms in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5D7G
Type: protein
Length: 1,201 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9H1Y0, Q676U5

Structure

x-ray diffraction · 7 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	263	—	Q9H1Y0
B	—	protein	39	—	Q676U5
C	—	protein	263	—	Q9H1Y0
D, H	—	protein	40	—	Q676U5
E	—	protein	260	—	Q9H1Y0
F	—	protein	40	—	Q676U5
G	—	protein	256	—	Q9H1Y0

Compared structures

5D7G · Structure of human ATG5 E122D-ATG16L1 complex at 3.0 Angstroms · the same entry in another collection · chain H against H, TM-score 1.00
Q9H1Y0 · AlphaFold monomer V2.0 prediction for autophagy protein 5 (Q9H1Y0) · a predicted model of the same protein · chain G against A, TM-score 0.99

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 Q9H1Y0
Every structure of UniProt Q676U5
Elsewhere: RCSB PDB 5D7G · PDBe 5D7G · UniProt Q9H1Y0 · UniProt Q676U5

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