Structure of PDB 4kp0 Chain A

Receptor sequence
>4kp0A (length=220) Species: 9606 (Homo sapiens) [Search protein sequence]
IIGGTECKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNFVLTAAHCAGRS
ITVTLGAHNITEEEDTWQKLEVIKQFRHPKYNTSTLHHDIMLLKLKEKAS
LTLAVGTLPFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACSH
FRDFDHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRSDAKPP
AVFTRISHYRPWINQILQAN
3D structure
PDB4kp0 Crystal structure of a complex of human chymase with its benzimidazole derived inhibitor
ChainA
Resolution2.8 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 K192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) H45 D89 K173 G174 D175 S176 G177
Enzyme Commision number 3.4.21.39: chymase.
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 KPK A H57 A190 F191 K192 G193 S195 Y215 G216 H45 A171 F172 K173 G174 S176 Y192 G193 PDBbind-CN: -logKd/Ki=8.65,Ki=2.24nM
BindingDB: IC50=22nM
Gene Ontology
Molecular Function
GO:0004175 endopeptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0042277 peptide binding
Biological Process
GO:0002003 angiotensin maturation
GO:0006508 proteolysis
GO:0006518 peptide metabolic process
GO:0016485 protein processing
GO:0022617 extracellular matrix disassembly
GO:0030163 protein catabolic process
GO:0030901 midbrain development
GO:0034769 basement membrane disassembly
GO:0045766 positive regulation of angiogenesis
GO:0050727 regulation of inflammatory response
GO:0071333 cellular response to glucose stimulus
GO:0140447 cytokine precursor processing
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0030141 secretory granule
GO:0036464 cytoplasmic ribonucleoprotein granule
GO:0043231 intracellular membrane-bounded organelle
GO:0062023 collagen-containing extracellular matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4kp0, PDBe:4kp0, PDBj:4kp0
PDBsum4kp0
PubMed24121339
UniProtP23946|CMA1_HUMAN Chymase (Gene Name=CMA1)

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