Structure of PDB 1pj8 Chain A

Receptor sequence
>1pj8A (length=279) Species: 37998 (Parengyodontium album) [Search protein sequence]
AAQTNAPWGLARISSTSPGTSTYYYDESAGQGSCVYVIDTGIEASHPEFE
GRAQMVKTYYYSSRDGNGHGTHCAGTVGSRTYGVAKKTQLFGVKVLDDNG
SGQYSTIIAGMDFVASDKNNRNCPKGVVASLSLGGGYSSSVNSAAARLQS
SGVMVAVAAGNNNADARNYSPASEPSVCTVGASDRYDRRSSFSNYGSVLD
IFGPGTSILSTWIGGSTRSISGTSMATPHVAGLAAYLMTLGKTTAASACR
YIADTANKGDLSNIPFGTVNLLAYNNYQA
3D structure
PDB1pj8 Structure of a ternary complex of proteinase K, mercury, and a substrate-analogue hexa-peptide at 2.2 A resolution
ChainA
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) D39 H69 N161 S224
Catalytic site (residue number reindexed from 1) D39 H69 N161 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 A N67 H69 N99 G100 L133 A158 G160 N161 S207 S219 I220 S221 G222 T223 S224 M225 N67 H69 N99 G100 L133 A158 G160 N161 S207 S219 I220 S221 G222 T223 S224 M225
BS02 HG A D39 H69 C73 S207 S219 D39 H69 C73 S207 S219
BS03 HG A H72 C73 M225 H72 C73 M225
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:1pj8, PDBe:1pj8, PDBj:1pj8
PDBsum1pj8
PubMed8811735
UniProtP06873|PRTK_PARAQ Proteinase K (Gene Name=PROK)

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