Brand  (β version)

PDB ID: 4FS3

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
0WD [[(2r,3s,4r,5r)-5-(3-aminocarbonyl-4h-pyridin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2r,3s,4r,5r)-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methyl hydrogen phosphate PoSSuM
0WE N-methyl-N-[(3-methyl-1-benzofuran-2-yl)methyl]-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthyridin-3-yl)propanamide PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 4FS3   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Crystal structure of Staphylococcus aureus enoyl-ACP reductase in complex with NADP and AFN-1252
Release Data : 2012-09-19
Compound :
mol_id molecule chains synonym
1 Enoyl-[acyl-carrier-protein] reductase [NADPH] FabI A ENR, NADPH-dependent enoyl-ACP reductase
ec: 1.3.1.10
Source :
mol_id organism_scientific expression_system
1 Staphylococcus aureus subsp. aureus  (taxid:282458) Escherichia coli  (taxid:562)
strain: MRSA252
gene: fabI, SAR0978
Authors : Kaplan, N., Yethon, J., Bardouniotis, E., Thalakada, R., Albert, M., Awrey, D.E., Romanov, V., Dorsey, M., Ramnauth, J., Clarke, T.E., Schmid, M.B., Berman, J., Pauls, H.W.
Keywords : Rossmann Fold, short chain dehydrogenase, NADPH binding, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 1.80 Å )
Citation :

Mode of Action, In Vitro Activity, and In Vivo Efficacy of AFN-1252, a Selective Antistaphylococcal FabI Inhibitor.

Kaplan, N.,Albert, M.,Awrey, D.  et al.
(2012)  Antimicrob.Agents Chemother.  56 : 5865 - 5874

PubMed: 22948878
DOI: 10.1128/AAC.01411-12

Reaction

Chain : A
UniProt : Q6GI75 (FABI_STAAR)
Reaction: EC: Evidence:
Physiological Direction:
a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] + H(+) + NADPH 1.3.1.39 -
-