1PJP
THE 2.2 A CRYSTAL STRUCTURE OF HUMAN CHYMASE IN COMPLEX WITH SUCCINYL-ALA-ALA-PRO-PHE-CHLOROMETHYLKETONE
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 | 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 | CST |
| Number of Residues | 3 |
| Details | CATALYTIC SITE |
| Chain | Residue |
| A | SER195 |
| A | HIS57 |
| A | ASP102 |
Functional Information from PROSITE/UniProt
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 |
| Chain | Residue | Details |
| A | ASP102 | |
| A | HIS57 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | SER195 | |
| A | GLY196 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | SER195 | |
| A | GLY193 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP102 | |
| A | SER195 | |
| A | HIS57 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP102 | |
| A | SER195 | |
| A | HIS57 | |
| A | GLY196 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP102 | |
| A | SER195 | |
| A | GLY193 | |
| A | HIS57 |
