Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P27169
ChainResidueDetails
AHIS115

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P27169
ChainResidueDetails
AGLU53
AASP54
AILE117
AASN168
AASP169
AASN224
AASP269
AASN270

site_idSWS_FT_FI3
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN50
AASN253
AASN270
AASN324

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

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

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon