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

4LA4

Crystal structure of native PnpB

Functional Information from GO Data
ChainGOidnamespacecontents
A0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
A0006091biological_processgeneration of precursor metabolites and energy
A0010181molecular_functionFMN binding
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016655molecular_functionoxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
A0018541molecular_functionp-benzoquinone reductase (NADPH) activity
A0046196biological_process4-nitrophenol catabolic process
A0050660molecular_functionflavin adenine dinucleotide binding
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
B0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
B0006091biological_processgeneration of precursor metabolites and energy
B0010181molecular_functionFMN binding
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016655molecular_functionoxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
B0018541molecular_functionp-benzoquinone reductase (NADPH) activity
B0046196biological_process4-nitrophenol catabolic process
B0050660molecular_functionflavin adenine dinucleotide binding
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|Ref.3
ChainResidueDetails
ASER11
ATHR84
ASER119
AHIS140
BSER11
BTHR84
BSER119
BHIS140

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0A8G6
ChainResidueDetails
ATYR13
BTYR13

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon