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5CDL

Proline dipeptidase from Deinococcus radiodurans (selenomethionine derivative)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0008235molecular_functionmetalloexopeptidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MN A 401
ChainResidue
AASP210
AASP221
AMSE222
ATHR223
AGLU328
APO4402

site_idAC2
Number of Residues9
Detailsbinding site for residue PO4 A 402
ChainResidue
AHIS285
AHIS292
AGLU314
AGLU328
AMN401
AHOH700
AASP210
AASP221
ATHR223

site_idAC3
Number of Residues8
Detailsbinding site for residue PO4 A 403
ChainResidue
AGLY122
AARG124
AGLU290
AGLU293
AGLY294
APO4404
AHOH516
AHOH578

site_idAC4
Number of Residues8
Detailsbinding site for residue PO4 A 404
ChainResidue
AASN26
AGLU92
AGLU94
ALEU120
APO4403
AHOH516
AHOH524
AHOH577

Functional Information from PROSITE/UniProt
site_idPS00491
Number of Residues13
DetailsPROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HSLGHgVGLeVHE
ChainResidueDetails
AHIS281-GLU293

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PDB entries from 2024-07-24

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