Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8RCZ

Structure of the enoyl-ACP reductase FabV from Pseudomonas aeruginosa with NADH cofactor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) activity
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0050343molecular_functiontrans-2-enoyl-CoA reductase (NADH) activity
A0051287molecular_functionNAD binding
B0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) activity
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0050343molecular_functiontrans-2-enoyl-CoA reductase (NADH) activity
B0051287molecular_functionNAD binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01838
ChainResidueDetails
ATYR237
BTYR237

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01838
ChainResidueDetails
AGLY50
BASP113
BLEU141
BTYR227
BLYS246
BVAL275
APHE76
AASP113
ALEU141
ATYR227
ALYS246
AVAL275
BGLY50
BPHE76

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Plays an important role in discriminating NADH against NADPH => ECO:0000255|HAMAP-Rule:MF_01838
ChainResidueDetails
AGLU77
BGLU77

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon