6SRE
Crystal Structure of Human Prolidase S202F variant expressed in the presence of chaperones
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 501 |
| Chain | Residue |
| A | ASP287 |
| A | HIS370 |
| A | GLU412 |
| A | GLU452 |
| A | MH2506 |
| A | GLY507 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | ASP125 |
| A | VAL126 |
| A | GLN127 |
| A | LYS114 |
| A | GLU115 |
| A | LYS118 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | ARG388 |
| A | HOH690 |
| A | HOH915 |
| A | HOH1030 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | PRO262 |
| A | ASP264 |
| A | HOH953 |
| B | SER8 |
| B | PHE9 |
| B | TRP10 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | PHE163 |
| A | ASP164 |
| A | GLY165 |
| A | ILE166 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue MH2 A 506 |
| Chain | Residue |
| A | TYR241 |
| A | ASP276 |
| A | ASP287 |
| A | THR289 |
| A | GLU412 |
| A | GLU452 |
| A | MN501 |
| A | GLY507 |
| A | PRO508 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue GLY A 507 |
| Chain | Residue |
| A | TYR241 |
| A | ASP276 |
| A | ASP287 |
| A | HIS370 |
| A | HIS377 |
| A | MN501 |
| A | MH2506 |
| A | PRO508 |
| A | HOH721 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue PRO A 508 |
| Chain | Residue |
| A | HIS255 |
| A | HIS366 |
| A | HIS377 |
| A | ARG398 |
| A | GLU412 |
| A | ARG450 |
| A | MH2506 |
| A | GLY507 |
| A | HOH742 |
| A | HOH855 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 501 |
| Chain | Residue |
| B | ASP287 |
| B | HIS370 |
| B | GLU412 |
| B | GLU452 |
| B | MH2502 |
| B | GLY508 |
| site_id | AD1 |
| Number of Residues | 9 |
| Details | binding site for residue MH2 B 502 |
| Chain | Residue |
| B | TYR241 |
| B | ASP276 |
| B | ASP287 |
| B | THR289 |
| B | GLU412 |
| B | GLU452 |
| B | MN501 |
| B | GLY508 |
| B | PRO509 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | SER134 |
| B | THR137 |
| B | SER138 |
| B | GLY349 |
| B | SER350 |
| B | VAL351 |
| B | ASP352 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | GLU387 |
| B | ARG388 |
| B | HOH758 |
| B | HOH790 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 505 |
| Chain | Residue |
| B | ARG311 |
| B | ARG335 |
| B | GLU339 |
| B | HOH1005 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 506 |
| Chain | Residue |
| A | ASP423 |
| A | GLU424 |
| A | HOH870 |
| B | LYS297 |
| B | PHE298 |
| B | HOH610 |
| B | HOH716 |
| B | HOH867 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 507 |
| Chain | Residue |
| B | ARG29 |
| B | ARG33 |
| B | PHE186 |
| B | HOH628 |
| B | HOH1020 |
| site_id | AD7 |
| Number of Residues | 9 |
| Details | binding site for residue GLY B 508 |
| Chain | Residue |
| B | ASP287 |
| B | HIS370 |
| B | HIS377 |
| B | MN501 |
| B | MH2502 |
| B | PRO509 |
| B | HOH998 |
| B | TYR241 |
| B | ASP276 |
| site_id | AD8 |
| Number of Residues | 8 |
| Details | binding site for residue PRO B 509 |
| Chain | Residue |
| B | HIS255 |
| B | HIS366 |
| B | HIS377 |
| B | ARG398 |
| B | MH2502 |
| B | GLY508 |
| B | HOH704 |
| B | HOH814 |
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 |
