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5D9T

Crystal structure of dehydroascorbate reductase (OsDHAR) from Oryza sativa L. japonica

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009636biological_processresponse to toxic substance
A0016491molecular_functionoxidoreductase activity
A0016740molecular_functiontransferase activity
A0033355biological_processascorbate glutathione cycle
A0045174molecular_functionglutathione dehydrogenase (ascorbate) activity
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue NA A 301
ChainResidue
ALYS47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:26775680
ChainResidueDetails
ACYS20

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:26775680, ECO:0007744|PDB:5D9W
ChainResidueDetails
ALYS8
AASP19
ALYS210

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9FWR4
ChainResidueDetails
ASER74
AVAL60
ALYS47

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:26775680, ECO:0007744|PDB:5D9X
ChainResidueDetails
ATRP207
AHIS160

221051

PDB entries from 2024-06-12

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