6H2Q
Crystal Structure of Arg184Gln mutant of Human Prolidase with Mn ions and LeuPro ligand
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 499 |
| Chain | Residue |
| A | ASP287 |
| A | HIS370 |
| A | GLU412 |
| A | GLU452 |
| A | MN500 |
| A | LEU506 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 500 |
| Chain | Residue |
| A | MN499 |
| A | LEU506 |
| A | ASP276 |
| A | ASP287 |
| A | GLU452 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | VAL129 |
| A | ASP130 |
| A | ILE132 |
| A | PHE163 |
| A | ASP164 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | GLN49 |
| A | ARG159 |
| A | GLU160 |
| A | ALA161 |
| A | HOH608 |
| A | HOH856 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | TRP10 |
| A | LYS120 |
| A | HOH618 |
| A | HOH625 |
| A | HOH688 |
| B | ASP264 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue LEU A 506 |
| Chain | Residue |
| A | TYR241 |
| A | HIS255 |
| A | ASP276 |
| A | ASP287 |
| A | HIS370 |
| A | HIS377 |
| A | GLU412 |
| A | GLU452 |
| A | MN499 |
| A | MN500 |
| A | PRO507 |
| A | HOH681 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue PRO A 507 |
| Chain | Residue |
| A | HIS255 |
| A | HIS366 |
| A | HIS377 |
| A | ARG398 |
| A | GLU412 |
| A | ARG450 |
| A | LEU506 |
| A | HOH742 |
| A | HOH766 |
| B | TRP107 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 499 |
| Chain | Residue |
| B | ASP287 |
| B | HIS370 |
| B | GLU412 |
| B | GLU452 |
| B | MN500 |
| B | LEU503 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue MN B 500 |
| Chain | Residue |
| B | ASP276 |
| B | ASP287 |
| B | GLU452 |
| B | MN499 |
| B | LEU503 |
| site_id | AD1 |
| Number of Residues | 12 |
| Details | binding site for residue LEU B 503 |
| Chain | Residue |
| B | TYR241 |
| B | HIS255 |
| B | ASP276 |
| B | ASP287 |
| B | HIS370 |
| B | HIS377 |
| B | GLU412 |
| B | GLU452 |
| B | MN499 |
| B | MN500 |
| B | PRO504 |
| B | HOH758 |
| site_id | AD2 |
| Number of Residues | 10 |
| Details | binding site for residue PRO B 504 |
| Chain | Residue |
| A | TRP107 |
| B | HIS255 |
| B | HIS366 |
| B | HIS377 |
| B | ARG398 |
| B | GLU412 |
| B | ARG450 |
| B | LEU503 |
| B | HOH683 |
| B | HOH713 |
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 | HIS366-ASP378 |
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 |
| B | HIS255 | |
| B | HIS377 | |
| B | ARG398 | |
| A | ARG398 | |
| A | HIS255 | |
| A | HIS377 |
| 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 | HIS370 | |
| A | GLU412 | |
| A | GLU452 | |
| B | ASP276 | |
| B | ASP287 | |
| B | HIS370 | |
| B | GLU412 | |
| B | GLU452 | |
| A | ASP276 | |
| A | ASP287 |
| 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 | ALA2 | |
| B | ALA2 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER167 | |
| B | SER167 |
