Structure of PDB 6nyy Chain B Binding Site BS01

Receptor Information
>6nyy Chain B (length=487) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VGETTAKVLKDEIDVKFKDVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKI
PKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVR
DLFALARKNAPCILFIDQIDAVGRKRGNFGGQSEQENTLNQLLVEMDGFN
TTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHLR
PLKLDSTLEKDKLARKLASLTPGFSGADVANVCNEAALIAARHLSDSINQ
KHFEQAIERVIGGLEKKTQVLQPEEKKTVAYHQAGHAVAGWYLEHADPLL
KVSIIPRGKGLGYAQYLPKEQYLYTKEQLLDRMCMTLGGRVSEEIFFGRI
TTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQGDMVLEKPYSEA
TARLIDDEVRILINDAYKRTVALLTEKKADVEKVALLLLEKEVLDKNDMV
ELLGPRPFAEKSTYEEFVEGTGSLDEDTSLPEGLKDW
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6nyy Unique Structural Features of the Mitochondrial AAA+ Protease AFG3L2 Reveal the Molecular Basis for Activity in Health and Disease.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		M380 F381 V382 F421
Binding residue
(residue number reindexed from 1)		M90 F91 V92 F129
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6nyy, PDBe:6nyy, PDBj:6nyy
PDBsum6nyy
PubMed31327635
UniProtQ9Y4W6|AFG32_HUMAN Mitochondrial inner membrane m-AAA protease component AFG3L2 (Gene Name=AFG3L2)

[Back to BioLiP]