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1PA2

ARABIDOPSIS THALIANA PEROXIDASE A2

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
A0009908biological_processflower development
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 Residues6
DetailsBINDING SITE FOR RESIDUE CA A 307
ChainResidue
AASP43
AVAL46
AGLY48
AASP50
ASER52
AHOH591

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 308
ChainResidue
AALA227
AASP229
ATHR170
AASP221
ATHR224

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 309
ChainResidue
AHOH483
AHOH563
AHOH748
AHOH749
AHOH762

site_idAC4
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 306
ChainResidue
AARG31
AALA34
ASER35
AARG38
APHE41
ASER73
APRO139
ASER140
APRO141
APHE152
ALEU162
ALEU165
ASER166
AALA168
AHIS169
AGLY172
AARG173
AALA174
AARG175
ASER245
AHOH353
AHOH356
AHOH605
AHOH633

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
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASN72

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING:
ChainResidueDetails
ASER73
AALA259
AGLY76
AASN78
AVAL80
AASN82
AHIS169
ALEU200
ASER251
AGLY254

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00297
ChainResidueDetails
ATHR199

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AGLY68

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:8977116
ChainResidueDetails
AARG31

site_idSWS_FT_FI6
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AGLY33
AASP43
ALEU165
AGLY177
ASER215
AALA227
AGLY241
ALEU297

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

223790

PDB entries from 2024-08-14

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