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3RVA

Crystal structure of organophosphorus acid anhydrolase from Alteromonas macleodii

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008235molecular_functionmetalloexopeptidase activity
A0008237molecular_functionmetallopeptidase activity
A0016787molecular_functionhydrolase activity
A0016795molecular_functionphosphoric triester hydrolase activity
A0016805molecular_functiondipeptidase activity
A0046872molecular_functionmetal ion binding
A0102009molecular_functionproline dipeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN A 452
ChainResidue
AASP244
AASP255
ATHR257
AGLU423
AMN453
AHOH460
AHOH857

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MN A 453
ChainResidue
ATHR382
AGLU384
AGLU423
AMN452
AHOH459
AHOH460
AASP255
AHIS339

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 A 454
ChainResidue
ALYS91
AHIS221
AHOH801

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI A 455
ChainResidue
ASER2
AGLN3
AHIS4
AASP76

Functional Information from PROSITE/UniProt
site_idPS00491
Number of Residues13
DetailsPROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HGIGHfLGLqVHD
ChainResidueDetails
AHIS335-ASP347

218853

PDB entries from 2024-04-24

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