Structure of PDB 4hrd Chain K

Receptor sequence
>4hrdK (length=212) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAA
DCQFWETWLGSQCRLHELREKERISVAAASKILSNLVYQYKGAGLSMGTM
ICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSV
EDALYLGKRSILAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKV
KEEEGSFNNVIG
3D structure
PDB4hrd Enzyme inhibition by hydroamination: design and mechanism of a hybrid carmaphycin-syringolin enone proteasome inhibitor.
ChainK
Resolution2.8 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 S131 D168 S171
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 OV1 K T1 A20 T21 G47 A49 T1 A20 T21 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:4hrd, PDBe:4hrd, PDBj:4hrd
PDBsum4hrd
PubMed24930969
UniProtP30656|PSB5_YEAST Proteasome subunit beta type-5 (Gene Name=PRE2)

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