Structure of PDB 4zar Chain A

Receptor sequence
>4zarA (length=279) Species: 37998 (Parengyodontium album) [Search protein sequence]
AAQTNAPWGLARISSTSPGTSTYYYDESAGQGSCVYVIDTGIEASHPEFE
GRAQMVKTYYYSSRDGNGHGTHCAGTVGSRTYGVAKKTQLFGVKVLDDNG
SGQYSTIIAGMDFVASDKNNRNCPKGVVASLSLGGGYSSSVNSAAARLQS
SGVMVAVAAGNNNADARNYSPASEPSVCTVGASDRYDRRSSFSNYGSVLD
IFGPGTDILSTWIGGSTRSISGTSMATPHVAGLAAYLMTLGKTTAASACR
YIADTANKGDLSNIPFGTVNLLAYNNYQA
3D structure
PDB4zar Inhibition of proteinase K by methoxysuccinyl-Ala-Ala-Pro-Ala-chloromethyl ketone. An x-ray study at 2.2-A resolution.
ChainA
Resolution1.15 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 H69 G100 G102 Y104 S132 L133 G134 G160 N161 S224 H69 G100 G102 Y104 S132 L133 G134 G160 N161 S224
BS02 CA A P175 V177 D200 P175 V177 D200
BS03 CA A T16 D260 T16 D260
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:4zar, PDBe:4zar, PDBj:4zar
PDBsum4zar
PubMed
UniProtP06873|PRTK_PARAQ Proteinase K (Gene Name=PROK)

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