Structure of PDB 4k1e Chain A

Receptor sequence
>4k1eA (length=223) Species: 9606 (Homo sapiens) [Search protein sequence]
IINGEDCSPHSQPWQAALVMENELFCSGVLVHPQWVLSAAHCFQNSYTIG
LGLHSLEADQEPGSQMVEASLSVRHPEYNRPLLANDLMLIKLDESVSESD
TIRSISIASQCPTAGNSCLVSGWGLLANGRMPTVLQCVNVSVVSEEVCSK
LYDPLYHPSMFCAGGGQDQKDSCNGDSGGPLICNGYLQGLVSFGKAPCGQ
VGVPGVYTNLCKFTEWIEKTVQA
3D structure
PDB4k1e Direct and indirect mechanisms of KLK4 inhibition revealed by structure and dynamics
ChainA
Resolution1.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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.-
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 F41 H57 L99 M151 Y172 L175 D189 S190 N192 G193 S195 S214 F215 G216 K217 A218 C220 F25 H41 L83 M131 Y152 L155 D171 S172 N174 G175 S177 S192 F193 G194 K195 A196 C198
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:4k1e, PDBe:4k1e, PDBj:4k1e
PDBsum4k1e
PubMed27767076
UniProtQ9Y5K2|KLK4_HUMAN Kallikrein-4 (Gene Name=KLK4)

[Back to BioLiP]