5LG6
Structure of the deglycosylated porcine aminopeptidase N ectodomain
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001525 | biological_process | angiogenesis |
A | 0001618 | molecular_function | virus receptor activity |
A | 0004177 | molecular_function | aminopeptidase activity |
A | 0005615 | cellular_component | extracellular space |
A | 0005737 | cellular_component | cytoplasm |
A | 0005886 | cellular_component | plasma membrane |
A | 0006508 | biological_process | proteolysis |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0030154 | biological_process | cell differentiation |
A | 0042277 | molecular_function | peptide binding |
A | 0043171 | biological_process | peptide catabolic process |
A | 0046718 | biological_process | symbiont entry into host cell |
A | 0046872 | molecular_function | metal ion binding |
A | 0070006 | molecular_function | metalloaminopeptidase activity |
B | 0001525 | biological_process | angiogenesis |
B | 0001618 | molecular_function | virus receptor activity |
B | 0004177 | molecular_function | aminopeptidase activity |
B | 0005615 | cellular_component | extracellular space |
B | 0005737 | cellular_component | cytoplasm |
B | 0005886 | cellular_component | plasma membrane |
B | 0006508 | biological_process | proteolysis |
B | 0008237 | molecular_function | metallopeptidase activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0030154 | biological_process | cell differentiation |
B | 0042277 | molecular_function | peptide binding |
B | 0043171 | biological_process | peptide catabolic process |
B | 0046718 | biological_process | symbiont entry into host cell |
B | 0046872 | molecular_function | metal ion binding |
B | 0070006 | molecular_function | metalloaminopeptidase activity |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIAHELAHQW |
Chain | Residue | Details |
A | VAL380-TRP389 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10095 |
Chain | Residue | Details |
A | GLU384 | |
B | GLU384 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P15144 |
Chain | Residue | Details |
A | GLY347 | |
B | GLY347 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22876187, ECO:0007744|PDB:4F5C |
Chain | Residue | Details |
A | HIS383 | |
A | HIS387 | |
A | GLU406 | |
B | HIS383 | |
B | HIS387 | |
B | GLU406 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P15144 |
Chain | Residue | Details |
A | TYR472 | |
B | TYR472 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Sulfotyrosine => ECO:0000255 |
Chain | Residue | Details |
A | TYR171 | |
B | TYR171 |
site_id | SWS_FT_FI6 |
Number of Residues | 20 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22876187, ECO:0007744|PDB:4F5C |
Chain | Residue | Details |
A | ASN82 | |
A | ASN736 | |
B | ASN82 | |
B | ASN124 | |
B | ASN229 | |
B | ASN237 | |
B | ASN314 | |
B | ASN328 | |
B | ASN506 | |
B | ASN622 | |
B | ASN646 | |
A | ASN124 | |
B | ASN736 | |
A | ASN229 | |
A | ASN237 | |
A | ASN314 | |
A | ASN328 | |
A | ASN506 | |
A | ASN622 | |
A | ASN646 |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN258 | |
A | ASN286 | |
A | ASN556 | |
A | ASN569 | |
B | ASN258 | |
B | ASN286 | |
B | ASN556 | |
B | ASN569 |