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4KP0

Crystal Structure of the human Chymase with TJK002

Functional Information from GO Data
ChainGOidnamespacecontents
A0002003biological_processangiotensin maturation
A0004175molecular_functionendopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0006518biological_processpeptide metabolic process
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016485biological_processprotein processing
A0016787molecular_functionhydrolase activity
A0022617biological_processextracellular matrix disassembly
A0030141cellular_componentsecretory granule
A0030163biological_processprotein catabolic process
A0030901biological_processmidbrain development
A0034769biological_processbasement membrane disassembly
A0036464cellular_componentcytoplasmic ribonucleoprotein granule
A0042277molecular_functionpeptide binding
A0043231cellular_componentintracellular membrane-bounded organelle
A0045766biological_processpositive regulation of angiogenesis
A0050727biological_processregulation of inflammatory response
A0062023cellular_componentcollagen-containing extracellular matrix
A0071333biological_processcellular response to glucose stimulus
A0140447biological_processcytokine precursor processing
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE KPK A 301
ChainResidue
AHIS57
AGLY216
AARG217
AASP78
AALA190
APHE191
ALYS192
AGLY193
ASER195
AVAL213
ASER214

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. SAfkGDSGGPLL
ChainResidueDetails
ASER189-LEU200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS57
AASP102
ASER195

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:2071582
ChainResidueDetails
AASN72

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN95

218853

PDB entries from 2024-04-24

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