3H5C
X-Ray Structure of Protein Z-Protein Z Inhibitor Complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0005788 | cellular_component | endoplasmic reticulum lumen |
A | 0007596 | biological_process | blood coagulation |
A | 0008201 | molecular_function | heparin binding |
A | 0010466 | biological_process | negative regulation of peptidase activity |
A | 0060046 | biological_process | regulation of acrosome reaction |
A | 0070062 | cellular_component | extracellular exosome |
A | 0097421 | biological_process | liver regeneration |
B | 0004252 | molecular_function | serine-type endopeptidase activity |
B | 0005509 | molecular_function | calcium ion binding |
B | 0006508 | biological_process | proteolysis |
Functional Information from PROSITE/UniProt
site_id | PS00010 |
Number of Residues | 12 |
Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CqDsiwgYtCtC |
Chain | Residue | Details |
B | CYS62-CYS73 |
site_id | PS00022 |
Number of Residues | 12 |
Details | EGF_1 EGF-like domain signature 1. CtCspGyeGSnC |
Chain | Residue | Details |
B | CYS71-CYS82 |
site_id | PS01186 |
Number of Residues | 12 |
Details | EGF_2 EGF-like domain signature 2. CtCspGYegsn....C |
Chain | Residue | Details |
B | CYS71-CYS82 | |
B | CYS110-CYS125 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 13 |
Details | MOD_RES: 4-carboxyglutamate => ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:2244898 |
Chain | Residue | Details |
B | PRO50 | |
B | CYS73 | |
B | GLY76 | |
B | GLU78 | |
B | GLU83 | |
B | CYS51 | |
B | GLN54 | |
B | HIS58 | |
B | GLY60 | |
B | GLN63 | |
B | ASP64 | |
B | TYR69 | |
B | THR70 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: (3R)-3-hydroxyaspartate => ECO:0000250 |
Chain | Residue | Details |
B | SER107 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | CARBOHYD: O-linked (Glc...) serine => ECO:0000269|PubMed:2129367, ECO:0000269|PubMed:2511201 |
Chain | Residue | Details |
B | GLY96 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20427285 |
Chain | Residue | Details |
B | LEU102 | |
B | GLU228 | |
B | PRO335 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19528533, ECO:0000269|PubMed:20427285 |
Chain | Residue | Details |
B | ALA236 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
B | MET309 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:20427285 |
Chain | Residue | Details |
A | ASN274 |