Structure of PDB 1ht3 Chain A

Receptor sequence
>1ht3A (length=279) Species: 37998 (Parengyodontium album) [Search protein sequence]
AAQTNAPWGLARISSTSPGTSTYYYDESAGQGSCVYVIDTGIEASHPEFE
GRAQMVKTYYYSSRDGNGHGTHCAGTVGSRTYGVVKKTQLFGVKVLDDNG
SGQYSTIIAGMDFVASDKNNRNCPKGVVASLSLGGGYSSSVNSAAARLQS
SGVMVAVAAGNNNADARNYSPASEPSVCTVGASDRYDRRSSFSNYGSVLD
IFGPGTSILSTWIGGSTRSISGTSMATPHVAGLAAYLMTLGKTTAASACR
YIADTANKGDLSNIPFGTVNLLAYNNYQA
3D structure
PDB1ht3 Mercury induced modifications in the stereochemistry of the active site through Cys-73 in a serine protease--crystal structure of the complex of a partially modified proteinase K with mercury at 1.8 A resolution
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) 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 HG A H72 C73 M225 H72 C73 M225
BS02 HG A D39 H69 C73 D39 H69 C73
BS03 CA A P175 V177 D200 P175 V177 D200
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:1ht3, PDBe:1ht3, PDBj:1ht3
PDBsum1ht3
PubMed11886076
UniProtP06873|PRTK_PARAQ Proteinase K (Gene Name=PROK)

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