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7K3U

X-ray crystallographic structure model of Lactococcus lactis prolidase mutant R293S

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0016805molecular_functiondipeptidase activity
A0046872molecular_functionmetal ion binding
A0102009molecular_functionproline dipeptidase activity
B0016787molecular_functionhydrolase activity
B0016805molecular_functiondipeptidase activity
B0046872molecular_functionmetal ion binding
B0102009molecular_functionproline dipeptidase activity
C0016787molecular_functionhydrolase activity
C0016805molecular_functiondipeptidase activity
C0046872molecular_functionmetal ion binding
C0102009molecular_functionproline dipeptidase activity
D0016787molecular_functionhydrolase activity
D0016805molecular_functiondipeptidase activity
D0046872molecular_functionmetal ion binding
D0102009molecular_functionproline dipeptidase activity
E0016787molecular_functionhydrolase activity
E0016805molecular_functiondipeptidase activity
E0046872molecular_functionmetal ion binding
E0102009molecular_functionproline dipeptidase activity
F0016787molecular_functionhydrolase activity
F0016805molecular_functiondipeptidase activity
F0046872molecular_functionmetal ion binding
F0102009molecular_functionproline dipeptidase activity
G0016787molecular_functionhydrolase activity
G0016805molecular_functiondipeptidase activity
G0046872molecular_functionmetal ion binding
G0102009molecular_functionproline dipeptidase activity
H0016787molecular_functionhydrolase activity
H0016805molecular_functiondipeptidase activity
H0046872molecular_functionmetal ion binding
H0102009molecular_functionproline dipeptidase activity
I0016787molecular_functionhydrolase activity
I0016805molecular_functiondipeptidase activity
I0046872molecular_functionmetal ion binding
I0102009molecular_functionproline dipeptidase activity
J0016787molecular_functionhydrolase activity
J0016805molecular_functiondipeptidase activity
J0046872molecular_functionmetal ion binding
J0102009molecular_functionproline dipeptidase activity
Functional Information from PROSITE/UniProt
site_idPS00491
Number of Residues13
DetailsPROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HSLGHgIGMdVHE
ChainResidueDetails
AHIS292-GLU304

238895

PDB entries from 2025-07-16

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