Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 401 |
Chain | Residue |
A | GLU23 |
A | GLN24 |
A | GLN222 |
A | VAL223 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 402 |
Chain | Residue |
A | GLN264 |
A | ARG265 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 403 |
Chain | Residue |
A | ASP272 |
A | ASP289 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 405 |
Chain | Residue |
A | ARG144 |
A | CYS311 |
A | HIS313 |
A | ZN413 |
A | TYR36 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 406 |
Chain | Residue |
A | ALA149 |
A | VAL152 |
A | HOH655 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 407 |
Chain | Residue |
A | GLY61 |
A | VAL62 |
A | VAL374 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 408 |
Chain | Residue |
A | PRO34 |
A | ASP47 |
A | THR48 |
A | PHE49 |
A | PRO118 |
A | HIS121 |
A | HOH531 |
A | HOH547 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 409 |
Chain | Residue |
A | ASP94 |
A | GLU368 |
A | ZN410 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 410 |
Chain | Residue |
A | ARG268 |
A | HIS367 |
A | ZN409 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 411 |
Chain | Residue |
A | ASP242 |
A | HIS306 |
A | GLU335 |
A | GLU349 |
A | ZN412 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 412 |
Chain | Residue |
A | ASP230 |
A | ASP242 |
A | THR244 |
A | GLU349 |
A | ZN411 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 413 |
Chain | Residue |
A | ASP37 |
A | ASP115 |
A | EDO405 |
A | HOH604 |
A | HOH663 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 414 |
Chain | Residue |
A | GLU50 |
A | HIS313 |
A | HOH598 |
A | HOH628 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 415 |
Chain | Residue |
A | CYS86 |
A | ASP251 |
A | HOH629 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 416 |
Chain | Residue |
A | HIS208 |
A | HOH637 |
A | HOH638 |
A | HOH648 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 417 |
Chain | Residue |
A | GLU71 |
A | HIS213 |
A | HOH606 |
A | HOH607 |
Functional Information from PROSITE/UniProt
site_id | PS00491 |
Number of Residues | 13 |
Details | PROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HRTGHgIGLcVHE |
Chain | Residue | Details |
A | HIS302-GLU314 | |