Structure of PDB 3prk Chain E

Receptor sequence
>3prkE (length=279) Species: 37998 (Parengyodontium album) [Search protein sequence]
AAQTNAPWGLARISSTSPGTSTYYYDESAGQGSCVYVIDTGIEASHPEFE
GRAQMVKTYYYSSRDGNGHGTHCAGTVGSRTYGVAKKTQLFGVKVLDDNG
SGQYSTIIAGMDFVASDKNNRNCPKGVVASLSLGGGYSSSVNSAAARLQS
SGVMVAVAAGNNNADARNYSPASEPSVCTVGASDRYDRRSSFSNYGSVLD
IFGPGTSILSTWIGGSTRSISGTSMATPHVAGLAAYLMTLGKTTAASACR
YIADTANKGDLSNIPFGTVNLLAYNNYQA
3D structure
PDB3prk Inhibition of proteinase K by methoxysuccinyl-Ala-Ala-Pro-Ala-chloromethyl ketone. An x-ray study at 2.2-A resolution.
ChainE
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S224
Catalytic site (residue number reindexed from 1) S224
Enzyme Commision number 3.4.21.64: peptidase K.
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 E H69 L96 G100 G102 Y104 S132 L133 G134 N161 S224 H69 L96 G100 G102 Y104 S132 L133 G134 N161 S224
BS02 CA E H69 P175 V177 D200 S224 H69 P175 V177 D200 S224
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:3prk, PDBe:3prk, PDBj:3prk
PDBsum3prk
PubMed1894649
UniProtP06873|PRTK_PARAQ Proteinase K (Gene Name=PROK)

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