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5EL8

The structure of DHAR1 from Arabidopsis thaliana

Functional Information from GO Data
ChainGOidnamespacecontents
A0000325cellular_componentplant-type vacuole
A0004364molecular_functionglutathione transferase activity
A0005507molecular_functioncopper ion binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006952biological_processdefense response
A0009507cellular_componentchloroplast
A0009570cellular_componentchloroplast stroma
A0009610biological_processresponse to symbiotic fungus
A0009636biological_processresponse to toxic substance
A0009753biological_processresponse to jasmonic acid
A0010043biological_processresponse to zinc ion
A0010193biological_processresponse to ozone
A0010731biological_processprotein glutathionylation
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016740molecular_functiontransferase activity
A0019852biological_processL-ascorbic acid metabolic process
A0033355biological_processascorbate glutathione cycle
A0034220biological_processmonoatomic ion transmembrane transport
A0034702cellular_componentmonoatomic ion channel complex
A0043903biological_processregulation of biological process involved in symbiotic interaction
A0045174molecular_functionglutathione dehydrogenase (ascorbate) activity
A0048046cellular_componentapoplast
A0070301biological_processcellular response to hydrogen peroxide
A0080151biological_processpositive regulation of salicylic acid mediated signaling pathway
A0098869biological_processcellular oxidant detoxification
A0140547biological_processacquisition of seed longevity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue GOL A 301
ChainResidue
ALYS8
AASP19
APRO21
AGLY206
ATRP207
ALYS210
AHOH449

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q65XA0
ChainResidueDetails
ACYS20

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q65XA0
ChainResidueDetails
ALYS8
AASP19
AHIS160
ATRP207
ALYS210

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|Ref.15, ECO:0007744|PDB:5ELG
ChainResidueDetails
ALYS47
AVAL60
ASER73

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: S-glutathionyl cysteine => ECO:0000269|PubMed:12077129, ECO:0000269|PubMed:16055689
ChainResidueDetails
ACYS20

224201

PDB entries from 2024-08-28

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