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Human M-aaa protease AFG3L2, substrate-bound

Analyse Human M-aaa protease AFG3L2, substrate-bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6NYY
Type: protein
Length: 2,894 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q9Y4W6
Ligands: ANP, ADP, ZN, MG

Structure

electron microscopy · 8 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	459	—	Q9Y4W6
B	—	protein	487	—	Q9Y4W6
C, D	—	protein	491	—	Q9Y4W6
E	—	protein	467	—	Q9Y4W6
F	—	protein	460	—	Q9Y4W6
G, H	—	protein	11	—	—
I	—	protein	9	—	—
J	—	protein	8	—	—

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 3 copies · chains B, C, D, E
ADP · Adenosine-5'-diphosphate · ligand · chains E
ZN · Zinc ion · metal · 6 copies · chains A, B, H, C, I, D, J, E, F
MG · Magnesium ion · metal · 3 copies · chains B, C, D, E

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

Compared structures

6NYY · human m-AAA protease AFG3L2, substrate-bound · the same entry in another collection · chain J against J, TM-score 1.00
Q9Y4W6 · AlphaFold monomer V2.0 prediction for AFG3-like protein 2 (Q9Y4W6) · a predicted model of the same protein · chain D against A, TM-score 0.98

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 Q9Y4W6
Elsewhere: RCSB PDB 6NYY · PDBe 6NYY · UniProt Q9Y4W6

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