Structure of PDB 6sju Chain F

Receptor sequence
>6sjuF (length=224) Species: 9606 (Homo sapiens) [Search protein sequence]
IIDGAPCARGSHPWQVALLSGNQLHCGGVLVNERWVLTAAHCKMNEYTVH
LGSDTLGDRRAQRIKASKSFRHPGYSTQTHVNDLMLVKLNSQARLSSMVK
KVRLPSRCEPPGTTCTVSGWGTTTSPDVTFPSDLMCVDVKLISPQDCTKV
YKDLLENSMLCAGIPDSKKNACNGDSGGPLVCRGTLQGLVSWGTFPCGQP
NDPGVYTQVCKFTKWINDTMKKHR
3D structure
PDB6sju Structural Studies on the Inhibitory Binding Mode of Aromatic Coumarinic Esters to Human Kallikrein-Related Peptidase 7.
ChainF
Resolution1.97 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H57 D102 N192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) H41 D83 N173 G174 D175 S176 G177
Enzyme Commision number 3.4.21.117: stratum corneum chymotryptic enzyme.
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 LFW F L40 H41 H57 N192 G193 S195 L24 H25 H41 N173 G174 S176
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0008233 peptidase activity
GO:0008236 serine-type peptidase activity
Biological Process
GO:0002803 positive regulation of antibacterial peptide production
GO:0006508 proteolysis
GO:0008544 epidermis development
GO:0022617 extracellular matrix disassembly
Cellular Component
GO:0001533 cornified envelope
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0030141 secretory granule
GO:0097209 epidermal lamellar body

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Cellular Component
External links
PDB RCSB:6sju, PDBe:6sju, PDBj:6sju
PDBsum6sju
PubMed32374603
UniProtP49862|KLK7_HUMAN Kallikrein-7 (Gene Name=KLK7)

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