Structure of PDB 4kel Chain A Binding Site BS01

Receptor Information

>4kel Chain A (length=223) Species: 9606 (Homo sapiens)

IINGEDCSPHSQPWQAALVMENELFCSGVLVHPQWVLSAAHCFQNSYTIG
LGLHSLEADQEPGSQMVEASLSVRHPEYNRPLLANDLMLIKLDESVSESD
TIRSISIASQCPTAGNSCLVSGWGLLANGRMPTVLQCVNVSVVSEEVCSK
LYDPLYHPSMFCAGGGQDQKDSCNGDSGGPLICNGYLQGLVSFGKAPCGQ
VGVPGVYTNLCKFTEWIEKTVQA

Ligand information

>4kel Chain B (length=14) Species: 4232 (Helianthus annuus)

GFCQRSIPPICFPN

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4kel KLK4 Inhibition by Cyclic and Acyclic Peptides: Structural and Dynamical Insights into Standard-Mechanism Protease Inhibitors.
• Resolution: 1.148 Å
• Binding residue (original residue number in PDB): F41 H57 L99 Y172 D189 S190 N192 G193 S195 S214 F215 G216 K217 A218 C220
• Binding residue (residue number reindexed from 1): F25 H41 L83 Y152 D171 S172 N174 G175 S177 S192 F193 G194 K195 A196 C198

Enzymatic activity

• Catalytic site (original residue number in PDB): H57 D102 N192 G193 D194 S195 G196
• Catalytic site (residue number reindexed from 1): H41 D86 N174 G175 D176 S177 G178
• 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

External links

• PDB: RCSB:4kel, PDBe:4kel, PDBj:4kel
• PDBsum: 4kel
• PubMed: 31058493
• UniProt: Q9Y5K2|KLK4_HUMAN Kallikrein-4 (Gene Name=KLK4)