Structure of PDB 1bjr Chain E

Receptor sequence

>1bjrE (length=279) Species: 37998 (Parengyodontium album)

AAQTNAPWGLARISSTSPGTSTYYYDESAGQGSCVYVIDTGIEASHPEFE
GRAQMVKTYYYSSRDGNGHGTHCAGTVGSRTYGVAKKTQLFGVKVLDDNG
SGQYSTIIAGMDFVASDKNNRNCPKGVVASLSLGGGYSSSVNSAAARLQS
SGVMVAVAAGNNNADARNYSPASEPSVCTVGASDRYDRRSSFSNYGSVLD
IFGPGTSILSTWIGGSTRSISGTSMATPHVAGLAAYLMTLGKTTAASACR
YIADTANKGDLSNIPFGTVNLLAYNNYQA

3D structure

• PDB: 1bjr Crystal structure of a complex formed between proteolytically-generated lactoferrin fragment and proteinase K.
• Chain: E
• Resolution: 2.44 Å

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	N67 H69 L96 N99 G100 S132 L133 G134 G135 V157 A158 A159 G160 N161 N162 Y169 P171 A172 W212 I220 G222 T223 S224 M225	N67 H69 L96 N99 G100 S132 L133 G134 G135 V157 A158 A159 G160 N161 N162 Y169 P171 A172 W212 I220 G222 T223 S224 M225
BS02	CA	E	R12 N257 L272 A273 Y274	R12 N257 L272 A273 Y274
BS03	CA	E	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

External links

• PDB: RCSB:1bjr, PDBe:1bjr, PDBj:1bjr
• PDBsum: 1bjr
• PubMed: 9741842
• UniProt: P06873|PRTK_PARAQ Proteinase K (Gene Name=PROK)