Structure of PDB 7px9 Chain A

Receptor sequence
>7px9A (length=463) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
PPSGYGVLLATHDDDTVDVFTSGRKMRLTCSPNIDAASLKKGQTVRLNEA
LTVVEAGTFEAVGEISTLREILADGHRALVVGHADEERVVWLADPLIPRK
LRPGDSLLVDTKAGYAFERIPKAEVEDLVLEEVPDVSYADIGGLSRQIEQ
IRDAVELPFLHKELYREYSLRPPKGVLLYGPPGCGKTLIAKAVANSLAKK
MAKSYFLNIKGPELLNKFVGETERHIRLIFQRAREKASEGTPVIVFFDEM
DSIFRTRGTGVVETTVVPQLLSEIDGVEGLENVIVIGASNREDMIDPAIL
RPGRLDVKIKIERPDAEAAQDIYSKYLTEFLPVHADDLAEFDGDRSACIK
AMIEKVVDRMYAEIDDNRFLEVTYANGDKEVMYFKDFNSGAMIQNVVDRA
KKNAIKSVLETGQPGLRIQHLLDSIVDEFAENEDLPNTTNPDDWARISGK
KGERIVYIRTLVT
3D structure
PDB7px9 Structural basis of prokaryotic ubiquitin-like protein engagement and translocation by the mycobacterial Mpa-proteasome complex.
ChainA
Resolution3.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 peptide A K340 V384 K217 V261
BS02 ATP A G255 P295 G296 C297 G298 K299 T300 L301 N416 I448 Y452 G516 Q520 G142 P182 G183 C184 G185 K186 T187 L188 N290 I322 Y326 G390 Q394
Gene Ontology
Molecular Function
GO:0004176 ATP-dependent peptidase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0042802 identical protein binding
GO:0140035 ubiquitin-like protein reader activity
Biological Process
GO:0010498 proteasomal protein catabolic process
GO:0010499 proteasomal ubiquitin-independent protein catabolic process
GO:0019941 modification-dependent protein catabolic process
GO:0030682 symbiont-mediated perturbation of host defenses
GO:0043335 protein unfolding
GO:0051409 response to nitrosative stress
GO:0052164 symbiont defense to host-produced reactive oxygen species
GO:0071732 cellular response to nitric oxide
Cellular Component
GO:0000502 proteasome complex
GO:0005886 plasma membrane
GO:0009274 peptidoglycan-based cell wall
GO:0022623 proteasome-activating nucleotidase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7px9, PDBe:7px9, PDBj:7px9
PDBsum7px9
PubMed35022401
UniProtP9WQN5|ARC_MYCTU Proteasome-associated ATPase (Gene Name=mpa)

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