1UWY
Crystal structure of human carboxypeptidase M
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004180 | molecular_function | carboxypeptidase activity |
| A | 0004181 | molecular_function | metallocarboxypeptidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006508 | biological_process | proteolysis |
| A | 0006518 | biological_process | peptide metabolic process |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009653 | biological_process | anatomical structure morphogenesis |
| A | 0009986 | cellular_component | cell surface |
| A | 0016485 | biological_process | protein processing |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0098552 | cellular_component | side of membrane |
Functional Information from PROSITE/UniProt
| site_id | PS00132 |
| Number of Residues | 23 |
| Details | CARBOXYPEPT_ZN_1 Zinc carboxypeptidases, zinc-binding region 1 signature. PeFkYvaNmHGdEtVGRelllhL |
| Chain | Residue | Details |
| A | PRO57-LEU79 |
| site_id | PS00133 |
| Number of Residues | 11 |
| Details | CARBOXYPEPT_ZN_2 Zinc carboxypeptidases, zinc-binding region 2 signature. HGGALVAsYPF |
| Chain | Residue | Details |
| A | HIS173-PHE183 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000305|PubMed:12457462 |
| Chain | Residue | Details |
| A | GLU264 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01379, ECO:0000269|PubMed:15066430, ECO:0007744|PDB:1UWY |
| Chain | Residue | Details |
| A | HIS66 | |
| A | GLU69 | |
| A | HIS173 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | SITE: Probable structural role => ECO:0000305|PubMed:12457462 |
| Chain | Residue | Details |
| A | GLU260 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | LIPID: GPI-anchor amidated serine => ECO:0000269|PubMed:12457462 |
| Chain | Residue | Details |
| A | SER406 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15066430 |
| Chain | Residue | Details |
| A | ASN21 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15066430, ECO:0000269|PubMed:19159218, ECO:0007744|PDB:1UWY |
| Chain | Residue | Details |
| A | ASN98 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 |
| Chain | Residue | Details |
| A | ASN147 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN346 | |
| A | ASN367 |
