Structure of PDB 5lzp Chain 0

Receptor sequence
>5lzp0 (length=215) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
SPEQAMRERSELARKGIARAKSVVALAYAGGVLFVAENPSRSLQKISELY
DRVGFAAAGKFNEFDNLRRGGIQFADTRGYAYDRRDVTGRQLANVYAQTL
GTIFTEQAKPYEVELCVAEVAHYGETKRPELYRITYDGSIADEPHFVVMG
GTTEPIANALKESYAENASLTDALRIAVAALRALGVASLEVAVLDANRPR
RAFRRITGSALQALL
3D structure
PDB5lzp Structural Analysis of the Bacterial Proteasome Activator Bpa in Complex with the 20S Proteasome.
Chain0
Resolution3.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.25.1: proteasome endopeptidase complex.
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 0 M13 D144 G145 S146 I147 M6 D137 G138 S139 I140
BS02 peptide 0 K28 K52 G66 K67 F68 E119 K21 K45 G59 K60 F61 E112
Gene Ontology
Molecular Function
GO:0004175 endopeptidase activity
GO:0004298 threonine-type endopeptidase activity
GO:0005515 protein binding
GO:0016787 hydrolase activity
Biological Process
GO:0010498 proteasomal protein catabolic process
GO:0019941 modification-dependent protein catabolic process
GO:0030682 symbiont-mediated perturbation of host defenses
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
GO:0051603 proteolysis involved in protein catabolic process
Cellular Component
GO:0000502 proteasome complex
GO:0005737 cytoplasm
GO:0005839 proteasome core complex
GO:0005886 plasma membrane
GO:0009274 peptidoglycan-based cell wall
GO:0019773 proteasome core complex, alpha-subunit complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5lzp, PDBe:5lzp, PDBj:5lzp
PDBsum5lzp
PubMed27839949
UniProtP9WHU1|PSA_MYCTU Proteasome subunit alpha (Gene Name=prcA)

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