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

3BA1

Structure of hydroxyphenylpyruvate reductase from coleus blumei

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005829cellular_componentcytosol
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0016618molecular_functionhydroxypyruvate reductase activity
A0030267molecular_functionglyoxylate reductase (NADPH) activity
A0047995molecular_functionhydroxyphenylpyruvate reductase activity
A0051287molecular_functionNAD binding
A0055114biological_processobsolete oxidation-reduction process
A0102742molecular_functionR(+)-3,4-dihydroxyphenyllactate:NADP+ oxidoreductase activity
Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VGIIGlGRIGlavaeraeafdcp.ISyFS
ChainResidueDetails
AVAL147-SER174

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AARG232
AGLU261

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AHIS279

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20445235
ChainResidueDetails
ASER174
AILE230
AASP256
ALEU152

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon