Pub. Date : 2009 Oct
PMID : 20024801
9 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex. | N-benzyloxycarbonylprolylprolinal | prolyl endopeptidase | Homo sapiens |
2 | We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex. | N-benzyloxycarbonylprolylprolinal | prolyl endopeptidase | Homo sapiens |
3 | We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex. | N-benzyloxycarbonylprolylprolinal | prolyl endopeptidase | Homo sapiens |
4 | We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex. | N-benzyloxycarbonylprolylprolinal | prolyl endopeptidase | Homo sapiens |
5 | We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex. | N-benzyloxycarbonylprolylprolinal | prolyl endopeptidase | Homo sapiens |
6 | We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex. | N-benzyloxycarbonylprolylprolinal | prolyl endopeptidase | Homo sapiens |
7 | We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex. | N-benzyloxycarbonylprolylprolinal | prolyl endopeptidase | Homo sapiens |
8 | We used the crystal structure of prolyl oligopeptidase (POP) with bound Z-pro-prolinal (ZPP) inhibitor (Protein Data Bank (PDB) structure 1QFS) to perform an intensive molecular dynamics study of the POP-ZPP complex. | N-benzyloxycarbonylprolylprolinal | prolyl endopeptidase | Homo sapiens |
9 | We performed 100 ns of simulation with the hemiacetal bond, through which the ZPP is bound to the POP, removed in order to better investigate the binding cavity environment. | N-benzyloxycarbonylprolylprolinal | prolyl endopeptidase | Homo sapiens |