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5IMA

Xanthomonas campestris Peroxiredoxin Q - Structure F2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005737cellular_componentcytoplasm
A0008379molecular_functionthioredoxin peroxidase activity
A0016209molecular_functionantioxidant activity
A0016491molecular_functionoxidoreductase activity
A0034599biological_processcellular response to oxidative stress
A0045454biological_processcell redox homeostasis
A0098869biological_processcellular oxidant detoxification
A0140824molecular_functionthioredoxin-dependent peroxiredoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue NA A 201
ChainResidue
AHIS30
AHIS33
ALEU128
ASER129
AHOH426

site_idAC2
Number of Residues4
Detailsbinding site for residue NA A 202
ChainResidue
ASER44
APHE83
AGLN87
AHOH303

site_idAC3
Number of Residues5
Detailsbinding site for residue NA A 203
ChainResidue
AALA137
AHOH361
AHOH416
AHOH461
AHOH514

site_idAC4
Number of Residues5
Detailsbinding site for residue FMT A 204
ChainResidue
AALA11
AASP14
ALYS116
AHOH319
AHOH336

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Cysteine sulfenic acid (-SOH) intermediate => ECO:0000305|PubMed:19477183, ECO:0000305|PubMed:27594682
ChainResidueDetails
ACSO48

219140

PDB entries from 2024-05-01

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