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1V04

serum paraoxonase by directed evolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004063molecular_functionaryldialkylphosphatase activity
A0004064molecular_functionarylesterase activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0009636biological_processresponse to toxic substance
A0016209molecular_functionantioxidant activity
A0016787molecular_functionhydrolase activity
A0034364cellular_componenthigh-density lipoprotein particle
A0046683biological_processresponse to organophosphorus
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
A0102007molecular_functionacyl-L-homoserine-lactone lactonohydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A1356
ChainResidue
AASP54
AILE117
AASP169
AHOH2010
AHOH2011
AHOH2053

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A1357
ChainResidue
AASP269
AASN270
APO41358
AHOH2009
AGLU53
AASN168
AASN224

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A1358
ChainResidue
AGLU53
AHIS115
AASN168
AASN224
AASP269
ATHR332
AVAL346
ACA1357

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P27169","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P27169","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 740
ChainResidueDetails
AGLU53metal ligand
AHIS115increase nucleophilicity, proton acceptor, proton donor, proton relay
AHIS134increase basicity, proton acceptor, proton donor
AASN168metal ligand
AASN224metal ligand
AASP269metal ligand
AASN270metal ligand

site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 15098021
ChainResidueDetails
AHIS134
AHIS115

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PDB entries from 2025-11-19

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