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6X1M

Lon protease proteolytic domain complexed with covalent boronic acid inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004176molecular_functionATP-dependent peptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005524molecular_functionATP binding
A0006508biological_processproteolysis
A0030163biological_processprotein catabolic process
B0004176molecular_functionATP-dependent peptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0005524molecular_functionATP binding
B0006508biological_processproteolysis
B0030163biological_processprotein catabolic process
C0004176molecular_functionATP-dependent peptidase activity
C0004252molecular_functionserine-type endopeptidase activity
C0005524molecular_functionATP binding
C0006508biological_processproteolysis
C0030163biological_processprotein catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue UKS A 1001
ChainResidue
AGLY767
AGLY853
APRO854
ASER855
AALA856
ALYS898
ALEU768
AALA769
ATRP770
ALEU778
AVAL780
AMET810
APRO850
AASP852

site_idAC2
Number of Residues13
Detailsbinding site for Di-peptide UKS B 1001 and SER B 855
ChainResidue
BALA769
BTRP770
BVAL780
BVAL844
BASP852
BGLY853
BPRO854
BALA856
BGLY857
BTHR880
BGLY881
BVAL892
BLYS898

Functional Information from PROSITE/UniProt
site_idPS01046
Number of Residues9
DetailsLON_SER ATP-dependent serine proteases, lon family, serine active site. DGPSAGCTI
ChainResidueDetails
AASP852-ILE860

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_03120
ChainResidueDetails
ASER855
ALYS898
BSER855
BLYS898
CSER855
CLYS898

224201

PDB entries from 2024-08-28

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