1K9X
Structure of Pyrococcus furiosus carboxypeptidase Apo-Yb
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004180 | molecular_function | carboxypeptidase activity |
A | 0004181 | molecular_function | metallocarboxypeptidase activity |
A | 0006508 | biological_process | proteolysis |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0050897 | molecular_function | cobalt ion binding |
B | 0004180 | molecular_function | carboxypeptidase activity |
B | 0004181 | molecular_function | metallocarboxypeptidase activity |
B | 0006508 | biological_process | proteolysis |
B | 0008237 | molecular_function | metallopeptidase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0050897 | molecular_function | cobalt ion binding |
C | 0004180 | molecular_function | carboxypeptidase activity |
C | 0004181 | molecular_function | metallocarboxypeptidase activity |
C | 0006508 | biological_process | proteolysis |
C | 0008237 | molecular_function | metallopeptidase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0050897 | molecular_function | cobalt ion binding |
D | 0004180 | molecular_function | carboxypeptidase activity |
D | 0004181 | molecular_function | metallocarboxypeptidase activity |
D | 0006508 | biological_process | proteolysis |
D | 0008237 | molecular_function | metallopeptidase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0050897 | molecular_function | cobalt ion binding |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. STVHEFGHAL |
Chain | Residue | Details |
A | SER266-LEU275 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01378 |
Chain | Residue | Details |
A | GLU270 | |
B | GLU270 | |
C | GLU270 | |
D | GLU270 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11839307 |
Chain | Residue | Details |
A | HIS269 | |
D | HIS269 | |
D | HIS273 | |
D | GLU299 | |
A | HIS273 | |
A | GLU299 | |
B | HIS269 | |
B | HIS273 | |
B | GLU299 | |
C | HIS269 | |
C | HIS273 | |
C | GLU299 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1i1i |
Chain | Residue | Details |
A | TYR423 | |
A | GLU299 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1i1i |
Chain | Residue | Details |
B | TYR423 | |
B | GLU299 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1i1i |
Chain | Residue | Details |
C | TYR423 | |
C | GLU299 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1i1i |
Chain | Residue | Details |
D | TYR423 | |
D | GLU299 |