Structure of PDB 1pjp Chain A Binding Site BS01

Receptor Information
>1pjp Chain A (length=226) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IIGGTECKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNFVLTAAHCAGRS
ITVTLGAHNITEEEDTWQKLEVIKQFRHPKYNTSTLHHDIMLLKLKEKAS
LTLAVGTLPFPSQKNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMD
PQACSHFRDFDHNLQLCVGNPRKTKSAFKGDSGGPLLCAGAAQGIVSYGR
SDAKPPAVFTRISHYQPWINQILQAN
Ligand information
Receptor-Ligand Complex Structure
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PDB1pjp The 2.2 A crystal structure of human chymase in complex with succinyl-Ala-Ala-Pro-Phe-chloromethylketone: structural explanation for its dipeptidyl carboxypeptidase specificity.
Resolution2.2 Å
Binding residue
(original residue number in PDB)
H57 L99 F191 K192 G193 S195 S214 Y215 G216
Binding residue
(residue number reindexed from 1)
H45 L86 F178 K179 G180 S182 S197 Y198 G199
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 K179 G180 D181 S182 G183
Enzyme Commision number 3.4.21.39: chymase.
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:1pjp, PDBe:1pjp, PDBj:1pjp
PDBsum1pjp
PubMed9931257
UniProtP23946|CMA1_HUMAN Chymase (Gene Name=CMA1)

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