Structure of PDB 6nyy Chain F Binding Site BS01

Receptor Information

>6nyy Chain F (length=460) Species: 9606 (Homo sapiens)

FSVGETTAKVLKDEIDVKFKDVAGCEEAKLEIMEFVNFLKNPKQYQDLGA
KIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPAR
VRDLFALARKNAPCILFIDQIDAVGRKRGQSEQENTLNQLLVEMDGFNTT
TNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHLRPL
KLDSTLEKDKLARKLASLTPGFSGADVANVCNEAALIAARHLSDSINQKH
FEQAIERVIGGLEKKTQVLQPEEKKTVAYHQAGHAVAGWYLEHADPLLKV
SIIPRGKGLGYAQYLPKEQYLYTKEQLLDRMCMTLGGRVSEEIFFGRITT
GAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQGDMVLEKPYSEATA
RLIDDEVRILINDAYKRTVALLTEKKADVEKVALLLLEKEVLDKNDMVEL
LGPRPFAEKS

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 6nyy Chain F Residue 801

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6nyy Unique Structural Features of the Mitochondrial AAA+ Protease AFG3L2 Reveal the Molecular Basis for Activity in Health and Disease.
• Resolution: 3.0 Å
• Binding residue (original residue number in PDB): H574 H578 D649
• Binding residue (residue number reindexed from 1): H280 H284 D355
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.4.24.-
  3.6.-.-

Gene Ontology

Molecular Function

• GO:0004176 ATP-dependent peptidase activity
• GO:0004222 metalloendopeptidase activity
• GO:0005524 ATP binding
• GO:0016887 ATP hydrolysis activity

Biological Process

• GO:0006508 proteolysis

Cellular Component

• GO:0016020 membrane

External links

• PDB: RCSB:6nyy, PDBe:6nyy, PDBj:6nyy
• PDBsum: 6nyy
• PubMed: 31327635
• UniProt: Q9Y4W6|AFG32_HUMAN Mitochondrial inner membrane m-AAA protease component AFG3L2 (Gene Name=AFG3L2)