Structure of PDB 6skb Chain A

Receptor sequence
>6skbA (length=223) Species: 9606 (Homo sapiens) [Search protein sequence]
LVHGGPCDKTSHPYQAALYTSGHLLCGGVLIHPLWVLTAAHCKKPNLQVF
LGKHNLGQQESSQEQSSVVRAVIHPDYDAASHDQDIMLLRLARPAKLSEL
IQPLPLERDCSAQTTSCHILGWGKTADGDFPDTIQCAYIHLVSREECEHA
YPGQITQNMLCAGDEKYGKDSCQGDSGGPLVCGDHLRGLVSWGDYPCGSK
ERPGVYTNVCRYTNWIQKTIQAK
3D structure
PDB6skb Design and development of a series of borocycles as selective, covalent kallikrein 5 inhibitors.
ChainA
Resolution1.84 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 L63 V65 A97 D102 Q192 G193 D194 S195
Catalytic site (residue number reindexed from 1) H41 L47 V49 A80 D85 Q173 G174 D175 S176
Enzyme Commision number 3.4.21.-
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 LH5 A L41 C42 H57 D189 S190 C191 Q192 G193 S195 V213 G216 D217 Y218 C220 L25 C26 H41 D170 S171 C172 Q173 G174 S176 V190 G193 D194 Y195 C197 PDBbind-CN: -logKd/Ki=7.70,IC50=19.9nM
BS02 RH5 A H57 D189 S190 C191 Q192 G193 S195 W215 G216 D217 Y218 C220 H41 D170 S171 C172 Q173 G174 S176 W192 G193 D194 Y195 C197
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:6skb, PDBe:6skb, PDBj:6skb
PDBsum6skb
PubMed31521475
UniProtQ92876|KLK6_HUMAN Kallikrein-6 (Gene Name=KLK6)

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