1KLT

CRYSTAL STRUCTURE OF PMSF-TREATED HUMAN CHYMASE AT 1.9 ANGSTROMS RESOLUTION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002003	biological_process	angiotensin maturation
A	0004175	molecular_function	endopeptidase activity
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005829	cellular_component	cytosol
A	0006508	biological_process	proteolysis
A	0006518	biological_process	peptide metabolic process
A	0008233	molecular_function	peptidase activity
A	0008236	molecular_function	serine-type peptidase activity
A	0016485	biological_process	protein processing
A	0016787	molecular_function	hydrolase activity
A	0022617	biological_process	extracellular matrix disassembly
A	0030141	cellular_component	secretory granule
A	0030163	biological_process	protein catabolic process
A	0030901	biological_process	midbrain development
A	0031012	cellular_component	extracellular matrix
A	0034769	biological_process	basement membrane disassembly
A	0036464	cellular_component	cytoplasmic ribonucleoprotein granule
A	0042277	molecular_function	peptide binding
A	0045766	biological_process	positive regulation of angiogenesis
A	0050727	biological_process	regulation of inflammatory response
A	0051604	biological_process	protein maturation
A	0071333	biological_process	cellular response to glucose stimulus
A	0140447	biological_process	cytokine precursor processing

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PMS A 400

Functional Information from PROSITE/UniProt

site_id	PS00134
Number of Residues	6
Details	TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC

Chain	Residue	Details
A	LEU53-CYS58

site_id	PS00135
Number of Residues	12
Details	TRYPSIN_SER Serine proteases, trypsin family, serine active site. SAfkGDSGGPLL

Chain	Residue	Details
A	SER189-LEU200

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	223
Details	Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	3
Details	Active site: {"description":"Charge relay system"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2071582","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j