5M4Q
Crystal Structure of Wild-Type Human Prolidase with Mn ions and Pro 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 | 7 |
Details | binding site for residue MN A 499 |
Chain | Residue |
A | ASP287 |
A | HIS370 |
A | GLU412 |
A | GLU452 |
A | MN500 |
A | OH501 |
A | HOH619 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue MN A 500 |
Chain | Residue |
A | THR289 |
A | GLU452 |
A | MN499 |
A | OH501 |
A | HOH877 |
A | ASP276 |
A | ASP287 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue OH A 501 |
Chain | Residue |
A | ASP276 |
A | ASP287 |
A | GLU412 |
A | GLU452 |
A | MN499 |
A | MN500 |
A | PRO504 |
A | HOH619 |
A | HOH877 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue PRO A 504 |
Chain | Residue |
A | HIS255 |
A | HIS366 |
A | HIS377 |
A | ARG398 |
A | GLU412 |
A | OH501 |
A | HOH619 |
A | HOH702 |
A | HOH734 |
B | TRP107 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue GOL A 505 |
Chain | Residue |
A | PHE9 |
A | TRP10 |
A | HOH603 |
A | HOH621 |
B | ASP264 |
site_id | AC6 |
Number of Residues | 9 |
Details | binding site for residue GOL A 506 |
Chain | Residue |
A | HIS330 |
A | ARG331 |
A | ASP334 |
A | HIS358 |
A | GLU391 |
A | PRO392 |
A | LEU394 |
A | HOH602 |
A | HOH605 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue GOL A 507 |
Chain | Residue |
A | THR152 |
A | GLU387 |
A | ARG388 |
A | HOH715 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue GOL A 508 |
Chain | Residue |
A | ALA342 |
A | HIS343 |
A | LEU347 |
A | SER348 |
A | HOH676 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue MN B 499 |
Chain | Residue |
B | ASP287 |
B | HIS370 |
B | GLU412 |
B | GLU452 |
B | MN500 |
B | OH501 |
B | HOH631 |
site_id | AD1 |
Number of Residues | 7 |
Details | binding site for residue MN B 500 |
Chain | Residue |
B | ASP276 |
B | ASP287 |
B | THR289 |
B | GLU452 |
B | MN499 |
B | OH501 |
B | HOH871 |
site_id | AD2 |
Number of Residues | 9 |
Details | binding site for residue OH B 501 |
Chain | Residue |
B | ASP276 |
B | ASP287 |
B | GLU412 |
B | GLU452 |
B | MN499 |
B | MN500 |
B | PRO504 |
B | HOH631 |
B | HOH871 |
site_id | AD3 |
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 | OH501 |
B | HOH631 |
B | HOH754 |
B | HOH800 |
site_id | AD4 |
Number of Residues | 9 |
Details | binding site for residue GOL B 505 |
Chain | Residue |
A | ASP264 |
B | PHE9 |
B | TRP10 |
B | LEU11 |
B | LYS120 |
B | HOH674 |
B | HOH752 |
B | HOH757 |
B | HOH965 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue GOL B 506 |
Chain | Residue |
B | GLY165 |
B | ILE166 |
B | SER167 |
B | HOH662 |
B | ASP164 |
site_id | AD6 |
Number of Residues | 10 |
Details | binding site for residue GOL B 507 |
Chain | Residue |
A | GLU227 |
A | HIS228 |
A | TYR231 |
A | HOH895 |
B | SER224 |
B | GLU227 |
B | HIS228 |
B | HOH632 |
B | HOH819 |
B | HOH834 |
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 |
A | HIS255 | |
A | HIS377 | |
A | ARG398 | |
B | HIS255 | |
B | HIS377 | |
B | ARG398 |
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 | ASP276 | |
B | GLU452 | |
A | ASP287 | |
A | HIS370 | |
A | GLU412 | |
A | GLU452 | |
B | ASP276 | |
B | ASP287 | |
B | HIS370 | |
B | GLU412 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER167 | |
B | SER167 |