Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1QO4

ARABIDOPSIS THALIANA PEROXIDASE A2 AT ROOM TEMPERATURE

Functional Information from GO Data
ChainGOidnamespacecontents
A0002215biological_processdefense response to nematode
A0004601molecular_functionperoxidase activity
A0005576cellular_componentextracellular region
A0005794cellular_componentGolgi apparatus
A0006979biological_processresponse to oxidative stress
A0009505cellular_componentplant-type cell wall
A0009908biological_processflower development
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
A0140825molecular_functionlactoperoxidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 375
ChainResidue
AASP43
AVAL46
AGLY48
AASP50
ASER52

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 376
ChainResidue
AASP229
ATHR170
AASP221
ATHR224
AALA227

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 374
ChainResidue
AARG31
AALA34
ASER35
AILE37
AARG38
APHE41
ASER73
APRO139
ASER140
APRO141
APHE152
AALA168
AHIS169
AGLY172
AARG173
AALA174
AARG175
AVAL178
ALEU243
ASER245
AHOH2009
AHOH2068

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. DLVALSGAHTF
ChainResidueDetails
AASP161-PHE171

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. GAslIRLhFHDC
ChainResidueDetails
AGLY33-CYS44

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Pyrrolidone carboxylic acid","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8977116","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1apx
ChainResidueDetails
AARG38
AHIS42
AASN70

245011

PDB entries from 2025-11-19

PDB statisticsPDBj update infoContact PDBjnumon