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3BAZ

Structure of hydroxyphenylpyruvate reductase from coleus blumei in complex with NADP+

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 PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE NAP A 500
ChainResidue
ALYS25
AALA202
ACYS203
APRO204
ATHR209
AILE230
AGLY231
AARG232
AASP256
AHIS279
AGLY281
AGLY151
AHOH511
AHOH513
AHOH589
AHOH592
AHOH610
AHOH611
ALEU152
AGLY153
AARG154
AILE155
ASER174
AARG175
ASER176

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

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