Structure of PDB 3gpj Chain K

Receptor sequence
>3gpjK (length=212) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAA
DCQFWETWLGSQCRLHELREKERISVAAASKILSNLVYQYKGAGLSMGTM
ICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSV
EDALYLGKRSILAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKV
KEEEGSFNNVIG
3D structure
PDB3gpj Synthetic and structural studies on syringolin A and B reveal critical determinants of selectivity and potency of proteasome inhibition
ChainK
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T1 D17 R19 K33 G47 S129 D166 S169
Catalytic site (residue number reindexed from 1) T1 D17 R19 K33 G47 S131 D168 S171
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 SY2 K T1 T21 K33 G47 A49 T1 T21 K33 G47 A49
Gene Ontology
Molecular Function
GO:0004298 threonine-type endopeptidase activity
Biological Process
GO:0051603 proteolysis involved in protein catabolic process
Cellular Component
GO:0005839 proteasome core complex

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Molecular Function
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Cellular Component
External links
PDB RCSB:3gpj, PDBe:3gpj, PDBj:3gpj
PDBsum3gpj
PubMed19359491
UniProtP30656|PSB5_YEAST Proteasome subunit beta type-5 (Gene Name=PRE2)

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