Structure of PDB 6o21 Chain A

Receptor sequence
>6o21A (length=220) Species: 9606 (Homo sapiens) [Search protein sequence]
IINGEDCSPHSQPWQAALVMENELFCSGVLVHPQWVLSAAHCFQNSYTIG
LGLHSLEEPGSQMVEASLSVRHPEYNRPLLANDLMLIKLDESVSESDTIR
SISIASQCPTAGNSCLVSGWGLLANGRMPTVLQCVNVSVVSEEVCSKLYD
PLYHPSMFCAGGGQDQKDSCNGDSGGPLICNGYLQGLVSFGKAPCGQVGV
PGVYTNLCKFTEWIEKTVQA
3D structure
PDB6o21 KLK4 Inhibition by Cyclic and Acyclic Peptides: Structural and Dynamical Insights into Standard-Mechanism Protease Inhibitors.
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) H57 D102 N192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) H41 D83 N171 G172 D173 S174 G175
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 peptide A H57 Y172 P174 L175 D189 S190 N192 G193 S195 S214 F215 G216 K217 C220 H41 Y149 P151 L152 D168 S169 N171 G172 S174 S189 F190 G191 K192 C195
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0005515 protein binding
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0022617 extracellular matrix disassembly
GO:0031214 biomineral tissue development
GO:0097186 amelogenesis
Cellular Component
GO:0005576 extracellular region
GO:0030141 secretory granule

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Biological Process
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Cellular Component
External links
PDB RCSB:6o21, PDBe:6o21, PDBj:6o21
PDBsum6o21
PubMed31058493
UniProtQ9Y5K2|KLK4_HUMAN Kallikrein-4 (Gene Name=KLK4)

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