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5CDV

Proline dipeptidase from Deinococcus radiodurans R1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0008235molecular_functionmetalloexopeptidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0046914molecular_functiontransition metal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MN A 401
ChainResidue
AASP210
AASP221
AMET222
ATHR223
AGLU328
APO4403

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 402
ChainResidue
AGLU328
AASP329
ALEU330
AASP221
AMET222
ATHR312

site_idAC3
Number of Residues9
Detailsbinding site for residue PO4 A 403
ChainResidue
AASP210
AASP221
ATHR223
AHIS285
AHIS292
AGLU314
AGLU328
AMN401
AHOH605

site_idAC4
Number of Residues11
Detailsbinding site for residue PO4 A 404
ChainResidue
AGLY121
AGLY122
AARG124
AGLU290
AGLU293
AGLY294
APO4405
AHOH536
AHOH543
AHOH546
AHOH683

site_idAC5
Number of Residues10
Detailsbinding site for residue PO4 A 405
ChainResidue
AASN26
AGLU92
AGLU94
ALEU120
APO4404
AHOH536
AHOH586
AHOH653
AHOH658
AHOH691

site_idAC6
Number of Residues4
Detailsbinding site for residue PO4 A 406
ChainResidue
APHE91
AGLU102
AARG105
AHOH730

site_idAC7
Number of Residues5
Detailsbinding site for residue PO4 A 407
ChainResidue
AARG28
AGLY216
AGLY217
AHOH502
AHOH703

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

224931

PDB entries from 2024-09-11

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