5X49
Crystal Structure of Human mitochondrial X-prolyl Aminopeptidase (XPNPEP3)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003094 | biological_process | glomerular filtration |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008235 | molecular_function | metalloexopeptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0016485 | biological_process | protein processing |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070006 | molecular_function | metalloaminopeptidase activity |
| B | 0003094 | biological_process | glomerular filtration |
| B | 0004177 | molecular_function | aminopeptidase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008235 | molecular_function | metalloexopeptidase activity |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0016485 | biological_process | protein processing |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070006 | molecular_function | metalloaminopeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MN A 601 |
| Chain | Residue |
| A | ASP342 |
| A | HIS424 |
| A | GLU451 |
| A | GLU475 |
| A | MN602 |
| A | 01B604 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MN A 602 |
| Chain | Residue |
| A | GLU475 |
| A | MN601 |
| A | 01B604 |
| A | ASP331 |
| A | ASP342 |
| A | THR344 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue 12P A 603 |
| Chain | Residue |
| A | LYS78 |
| A | TYR123 |
| A | ARG242 |
| A | LEU243 |
| A | ILE246 |
| A | LEU440 |
| A | GLN443 |
| A | DMS606 |
| A | HOH926 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue 01B A 604 |
| Chain | Residue |
| A | TYR300 |
| A | PRO301 |
| A | HIS314 |
| A | ASP331 |
| A | ASP342 |
| A | HIS424 |
| A | HIS431 |
| A | GLU451 |
| A | GLU475 |
| A | MN601 |
| A | MN602 |
| A | DMS607 |
| B | ILE111 |
| B | HOH858 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue DMS A 605 |
| Chain | Residue |
| A | LEU313 |
| A | HIS420 |
| A | GLU451 |
| A | ARG473 |
| A | HOH798 |
| B | TRP163 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 606 |
| Chain | Residue |
| A | GLU71 |
| A | LEU74 |
| A | 12P603 |
| A | HOH779 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 607 |
| Chain | Residue |
| A | HIS421 |
| A | ARG438 |
| A | GLU451 |
| A | 01B604 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 608 |
| Chain | Residue |
| A | LEU298 |
| B | MET107 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 601 |
| Chain | Residue |
| B | ASP342 |
| B | HIS424 |
| B | GLU451 |
| B | GLU475 |
| B | MN602 |
| B | 01B604 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 602 |
| Chain | Residue |
| B | ASP331 |
| B | ASP342 |
| B | THR344 |
| B | GLU475 |
| B | MN601 |
| B | 01B604 |
| site_id | AD2 |
| Number of Residues | 10 |
| Details | binding site for residue 12P B 603 |
| Chain | Residue |
| B | LYS78 |
| B | TYR123 |
| B | ARG242 |
| B | LEU243 |
| B | ILE246 |
| B | LEU440 |
| B | GLN443 |
| B | DMS606 |
| B | HOH763 |
| B | HOH895 |
| site_id | AD3 |
| Number of Residues | 14 |
| Details | binding site for residue 01B B 604 |
| Chain | Residue |
| A | ILE111 |
| B | TYR300 |
| B | PRO301 |
| B | HIS314 |
| B | ASP331 |
| B | ASP342 |
| B | HIS424 |
| B | HIS431 |
| B | GLU451 |
| B | GLU475 |
| B | MN601 |
| B | MN602 |
| B | DMS607 |
| B | HOH873 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue DMS B 605 |
| Chain | Residue |
| A | TRP163 |
| B | LEU313 |
| B | HIS420 |
| B | GLU451 |
| B | ARG473 |
| B | HOH880 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 606 |
| Chain | Residue |
| B | GLU71 |
| B | LEU74 |
| B | 12P603 |
| B | HOH1093 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue DMS B 607 |
| Chain | Residue |
| B | ARG438 |
| B | GLU451 |
| B | 01B604 |
| B | HOH925 |
| A | HOH1072 |
| B | HIS421 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 608 |
| Chain | Residue |
| A | HOH726 |
| B | LEU298 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28476889","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5X49","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28476889","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25609706","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5X49","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
