4KX9
Crystal structure of human aminopeptidase A complexed with arginine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001525 | biological_process | angiogenesis |
A | 0002003 | biological_process | angiotensin maturation |
A | 0003081 | biological_process | regulation of systemic arterial blood pressure by renin-angiotensin |
A | 0004177 | molecular_function | aminopeptidase activity |
A | 0005615 | cellular_component | extracellular space |
A | 0005737 | cellular_component | cytoplasm |
A | 0005765 | cellular_component | lysosomal membrane |
A | 0005886 | cellular_component | plasma membrane |
A | 0005903 | cellular_component | brush border |
A | 0006508 | biological_process | proteolysis |
A | 0007267 | biological_process | cell-cell signaling |
A | 0008217 | biological_process | regulation of blood pressure |
A | 0008233 | molecular_function | peptidase activity |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008283 | biological_process | cell population proliferation |
A | 0009897 | cellular_component | external side of plasma membrane |
A | 0016324 | cellular_component | apical plasma membrane |
A | 0016477 | biological_process | cell migration |
A | 0031410 | cellular_component | cytoplasmic vesicle |
A | 0032835 | biological_process | glomerulus development |
A | 0042277 | molecular_function | peptide binding |
A | 0043171 | biological_process | peptide catabolic process |
A | 0045177 | cellular_component | apical part of cell |
A | 0046872 | molecular_function | metal ion binding |
A | 0070006 | molecular_function | metalloaminopeptidase activity |
A | 0070062 | cellular_component | extracellular exosome |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVAHELVHQW |
Chain | Residue | Details |
A | VAL390-TRP399 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXD |
Chain | Residue | Details |
A | GLU394 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB |
Chain | Residue | Details |
A | GLU223 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD |
Chain | Residue | Details |
A | GLY357 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD |
Chain | Residue | Details |
A | HIS393 | |
A | HIS397 | |
A | GLU416 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD |
Chain | Residue | Details |
A | ARG887 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | SITE: Binds calcium which modulates its enzyme activity => ECO:0000269|PubMed:23888046 |
Chain | Residue | Details |
A | ASP221 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | SITE: Transition state stabilizer => ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD |
Chain | Residue | Details |
A | TYR479 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine; atypical => ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7 |
Chain | Residue | Details |
A | ASN98 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN124 | |
A | ASN773 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD |
Chain | Residue | Details |
A | ASN197 | |
A | ASN678 | |
A | ASN801 | |
A | ASN828 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD |
Chain | Residue | Details |
A | ASN324 | |
A | ASN763 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXB, ECO:0007744|PDB:4KXC |
Chain | Residue | Details |
A | ASN340 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX7, ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KX9, ECO:0007744|PDB:4KXA, ECO:0007744|PDB:4KXC, ECO:0007744|PDB:4KXD |
Chain | Residue | Details |
A | ASN554 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN589 |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23888046, ECO:0007744|PDB:4KX8, ECO:0007744|PDB:4KXD |
Chain | Residue | Details |
A | ASN597 |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN607 |