2OKN
Crystal Strcture of Human Prolidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004181 | molecular_function | metallocarboxypeptidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0006508 | biological_process | proteolysis |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0016805 | molecular_function | dipeptidase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0030574 | biological_process | collagen catabolic process |
| A | 0043069 | biological_process | negative regulation of programmed cell death |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070006 | molecular_function | metalloaminopeptidase activity |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0102009 | molecular_function | proline dipeptidase activity |
| B | 0004181 | molecular_function | metallocarboxypeptidase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0006508 | biological_process | proteolysis |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0016805 | molecular_function | dipeptidase activity |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0030574 | biological_process | collagen catabolic process |
| B | 0043069 | biological_process | negative regulation of programmed cell death |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070006 | molecular_function | metalloaminopeptidase activity |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0102009 | molecular_function | proline dipeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 495 |
| Chain | Residue |
| A | ASP288 |
| A | HIS371 |
| A | GLU413 |
| A | GLU453 |
| A | MN496 |
| A | PI501 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 496 |
| Chain | Residue |
| A | MN495 |
| A | PI501 |
| A | ASP277 |
| A | ASP288 |
| A | GLU453 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 495 |
| Chain | Residue |
| B | ASP288 |
| B | HIS371 |
| B | GLU413 |
| B | GLU453 |
| B | MN496 |
| B | PI502 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN B 496 |
| Chain | Residue |
| B | ASP277 |
| B | ASP288 |
| B | GLU453 |
| B | MN495 |
| B | PI502 |
| B | HOH567 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PI A 501 |
| Chain | Residue |
| A | ASP277 |
| A | ASP288 |
| A | HIS371 |
| A | HIS378 |
| A | GLU413 |
| A | GLU453 |
| A | MN495 |
| A | MN496 |
| A | HOH503 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PI B 502 |
| Chain | Residue |
| B | HIS256 |
| B | ASP277 |
| B | ASP288 |
| B | HIS371 |
| B | HIS378 |
| B | GLU413 |
| B | GLU453 |
| B | MN495 |
| B | MN496 |
| B | HOH567 |
| B | HOH573 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PI B 503 |
| Chain | Residue |
| B | VAL387 |
| B | HIS403 |
| B | GLN405 |
| B | HOH563 |
Functional Information from PROSITE/UniProt
| site_id | PS00491 |
| Number of Residues | 13 |
| Details | PROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HGLGHfLGIdVHD |
| Chain | Residue | Details |
| A | HIS367-ASP379 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28677335, ECO:0007744|PDB:5M4J, ECO:0007744|PDB:5M4L |
| Chain | Residue | Details |
| A | TYR257 | |
| A | ASP379 | |
| A | THR400 | |
| B | TYR257 | |
| B | ASP379 | |
| B | THR400 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:28677335, ECO:0007744|PDB:5M4G, ECO:0007744|PDB:5M4L, ECO:0007744|PDB:5M4Q |
| Chain | Residue | Details |
| A | PHE372 | |
| A | PRO414 | |
| A | GLU454 | |
| B | MET278 | |
| B | ILE289 | |
| B | PHE372 | |
| B | PRO414 | |
| B | GLU454 | |
| A | MET278 | |
| A | ILE289 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895 |
| Chain | Residue | Details |
| A | ALA4 | |
| B | ALA4 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | LYS169 | |
| B | LYS169 |
