Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5D9V

Crystal structure of oxidized 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 Residues2
Detailsbinding site for residue CA A 301
ChainResidue
ALYS197
ALYS200

site_idAC2
Number of Residues4
Detailsbinding site for residue CA A 302
ChainResidue
AHIS13
APRO14
AASP15
ATHR16

site_idAC3
Number of Residues3
Detailsbinding site for residue PEG A 303
ChainResidue
AGLN162
AGLU166
ALYS200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:26775680
ChainResidueDetails
AOCS20

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
ALYS47
AVAL60
ASER74

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

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon