Structure of PDB 6o21 Chain A Binding Site BS01
Receptor Information
>6o21 Chain A (length=220) Species:
9606
(Homo sapiens) [
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IINGEDCSPHSQPWQAALVMENELFCSGVLVHPQWVLSAAHCFQNSYTIG
LGLHSLEEPGSQMVEASLSVRHPEYNRPLLANDLMLIKLDESVSESDTIR
SISIASQCPTAGNSCLVSGWGLLANGRMPTVLQCVNVSVVSEEVCSKLYD
PLYHPSMFCAGGGQDQKDSCNGDSGGPLICNGYLQGLVSFGKAPCGQVGV
PGVYTNLCKFTEWIEKTVQA
Ligand information
>6o21 Chain B (length=11) Species:
4232
(Helianthus annuus) [
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GFCQRPICFPN
Receptor-Ligand Complex Structure
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PDB
6o21
KLK4 Inhibition by Cyclic and Acyclic Peptides: Structural and Dynamical Insights into Standard-Mechanism Protease Inhibitors.
Resolution
1.15 Å
Binding residue
(original residue number in PDB)
H57 Y172 P174 L175 D189 S190 N192 G193 S195 S214 F215 G216 K217 C220
Binding residue
(residue number reindexed from 1)
H41 Y149 P151 L152 D168 S169 N171 G172 S174 S189 F190 G191 K192 C195
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.-
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:6o21
,
PDBe:6o21
,
PDBj:6o21
PDBsum
6o21
PubMed
31058493
UniProt
Q9Y5K2
|KLK4_HUMAN Kallikrein-4 (Gene Name=KLK4)
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