Structure of PDB 2bdi Chain G

Receptor sequence
>2bdiG (length=223) Species: 9606 (Homo sapiens) [Search protein sequence]
IINGEDCSPHSQPWQAALVMENELFCSGVLVHPQWVLSAAHCFQNSYTIG
LGLHSLEADQEPGSQMVEASLSVRHPEYNRPLLANDLMLIKLDESVSESD
TIRSISIASQCPTAGNSCLVSGWGLLANGRMPTVLQCVNVSVVSEEVCSK
LYDPLYHPSMFCAGGGQDQKDSCNGDSGGPLICNGYLQGLVSFGKAPCGQ
VGVPGVYTNLCKFTEWIEKTVQA
3D structure
PDB2bdi Crystal structures of human tissue kallikrein 4: activity modulation by a specific zinc binding site.
ChainG
Resolution3.0 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 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 PBZ G D189 S190 C191 N192 F215 C220 D171 S172 C173 N174 F193 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

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Biological Process

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Cellular Component
External links
PDB RCSB:2bdi, PDBe:2bdi, PDBj:2bdi
PDBsum2bdi
PubMed16950394
UniProtQ9Y5K2|KLK4_HUMAN Kallikrein-4 (Gene Name=KLK4)

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