Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
B | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | binding site for residue K A 401 |
Chain | Residue |
A | GLU293 |
A | GLU294 |
A | HOH524 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ACT B 401 |
Chain | Residue |
A | VAL256 |
A | GLY261 |
B | SER277 |
B | HOH510 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue ACT B 402 |
Chain | Residue |
B | GLY261 |
B | HOH512 |
A | SER277 |
B | VAL256 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue K B 403 |
Chain | Residue |
B | GLU293 |
B | GLU294 |
B | HOH526 |
Functional Information from PROSITE/UniProt
site_id | PS00280 |
Number of Residues | 19 |
Details | BPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FvyGGClgnknnYlreeeC |
Chain | Residue | Details |
A | PHE278-CYS296 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 100 |
Details | Domain: {"description":"BPTI/Kunitz inhibitor 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00031","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Site: {"description":"Reactive bond","evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |