Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001869 | biological_process | negative regulation of complement activation, lectin pathway |
A | 0004222 | molecular_function | metalloendopeptidase activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0006508 | biological_process | proteolysis |
A | 0008233 | molecular_function | peptidase activity |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0010765 | biological_process | positive regulation of sodium ion transport |
A | 0045959 | biological_process | negative regulation of complement activation, classical pathway |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 500 |
Chain | Residue |
A | HOH1061 |
A | HIS176 |
A | HIS180 |
A | HIS186 |
A | TYR216 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 501 |
Chain | Residue |
A | ARG253 |
A | GLY255 |
A | THR257 |
A | ASP285 |
A | GLY287 |
A | ASP290 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 502 |
Chain | Residue |
A | GLY288 |
A | ASP290 |
A | THR327 |
A | GLU329 |
A | HOH1028 |
A | HOH1252 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 503 |
Chain | Residue |
A | GLY334 |
A | GLY336 |
A | ASP338 |
A | GLY351 |
A | ALA353 |
A | ASP356 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CA A 504 |
Chain | Residue |
A | GLY352 |
A | ALA353 |
A | GLY354 |
A | ASP356 |
A | GLY369 |
A | GLY370 |
A | ALA371 |
A | ASP374 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 505 |
Chain | Residue |
A | GLY370 |
A | GLY372 |
A | ASP374 |
A | GLN399 |
A | ASP400 |
A | HOH1160 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 506 |
Chain | Residue |
A | ASN343 |
A | VAL345 |
A | ASN347 |
A | GLY360 |
A | LEU362 |
A | ASP365 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 507 |
Chain | Residue |
A | GLY361 |
A | GLY363 |
A | ASP365 |
A | GLU383 |
A | ASP390 |
A | HOH1313 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 508 |
Chain | Residue |
A | ASP446 |
A | SER448 |
A | ASP450 |
A | HIS452 |
A | ASP454 |
site_id | CAT |
Number of Residues | 5 |
Details | THE ZINC ION AT THE BOTTOM OF CATALYTIC CLEFT HAS FIVE LIGANDS |
Chain | Residue |
A | HIS176 |
A | HIS180 |
A | HIS186 |
A | TYR216 |
A | HOH1061 |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TLTHEIGHTL |
Chain | Residue | Details |
A | THR173-LEU182 | |
site_id | PS00330 |
Number of Residues | 19 |
Details | HEMOLYSIN_CALCIUM Hemolysin-type calcium-binding region signature. DiLygglGaDqLwGGagaD |
Chain | Residue | Details |
A | ASP356-ASP374 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: |
Chain | Residue | Details |
A | GLU177 | |
site_id | SWS_FT_FI2 |
Number of Residues | 41 |
Details | BINDING: |
Chain | Residue | Details |
A | HIS176 | |
A | ASP290 | |
A | THR327 | |
A | GLU329 | |
A | GLY334 | |
A | GLY336 | |
A | ASP338 | |
A | ASN343 | |
A | VAL345 | |
A | ASN347 | |
A | GLY351 | |
A | HIS180 | |
A | GLY352 | |
A | ALA353 | |
A | GLY354 | |
A | ASP356 | |
A | GLY360 | |
A | GLY361 | |
A | LEU362 | |
A | GLY363 | |
A | ASP365 | |
A | GLY369 | |
A | HIS186 | |
A | GLY370 | |
A | ALA371 | |
A | GLY372 | |
A | ASP374 | |
A | GLU383 | |
A | ASP390 | |
A | ASP400 | |
A | ASP446 | |
A | SER448 | |
A | ASP450 | |
A | ARG253 | |
A | HIS452 | |
A | ASP454 | |
A | GLY255 | |
A | THR257 | |
A | ASP285 | |
A | GLY287 | |
A | GLY288 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1hfs |
Chain | Residue | Details |
A | GLU177 | |
A | GLU194 | |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1hfs |
Chain | Residue | Details |
A | GLU177 | |