1XVW

Crystal Structure of AhpE from Mycobacterium tuberculosis, a 1-Cys peroxiredoxin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004601	molecular_function	peroxidase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008379	molecular_function	thioredoxin peroxidase activity
A	0016209	molecular_function	antioxidant activity
A	0016491	molecular_function	oxidoreductase activity
A	0034599	biological_process	cellular response to oxidative stress
A	0045454	biological_process	cell redox homeostasis
A	0051409	biological_process	response to nitrosative stress
A	0051920	molecular_function	peroxiredoxin activity
A	0098869	biological_process	cellular oxidant detoxification
B	0003824	molecular_function	catalytic activity
B	0004601	molecular_function	peroxidase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008379	molecular_function	thioredoxin peroxidase activity
B	0016209	molecular_function	antioxidant activity
B	0016491	molecular_function	oxidoreductase activity
B	0034599	biological_process	cellular response to oxidative stress
B	0045454	biological_process	cell redox homeostasis
B	0051409	biological_process	response to nitrosative stress
B	0051920	molecular_function	peroxiredoxin activity
B	0098869	biological_process	cellular oxidant detoxification

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Cysteine sulfenic acid (-SOH) intermediate","evidences":[{"source":"PubMed","id":"15701515","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19737009","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1XVW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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