3G11: E. coli FabF(C163Q)

Structure of E. coli FabF(C163Q) in complex with dihydrophenyl platensimycin. Determined by X-ray diffraction at 2.0 Å resolution. Released 17 Mar 2009.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Escherichia coli
Chains
1
Atoms
3,450
Mol. weight
45.18 kDa
Ligands
P9C
Released
17 Mar 2009

Explore 3G11 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3G11 contains 22 α-helices and 26 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 22 helices, 26 β-strands

ElementResiduesLengthSheet
β-strand5-1391
β-strand1412
β-strand1712
α-helix20-289
β-strand34-3633
β-strand49-5133
α-helix52-532
α-helix64-674
α-helix72-8817
α-helix94-974
β-strand100-10561
α-helix111-12414
α-helix126-1283
α-helix133-1375
α-helix141-15010
β-strand156-15721
α-helix162-1643
α-helix165-17915
β-strand184-19181
α-helix196-2049
β-strand20814
α-helix215-2184
β-strand22315
β-strand22914
β-strand23116
β-strand23213
β-strand234-24291
α-helix243-2486
β-strand255-264101
α-helix277-29014
α-helix294-2963
β-strand299-30131
α-helix308-32215
α-helix323-3275
β-strand330-33231
α-helix335-3384
β-strand34016
α-helix342-3443
α-helix345-35915
β-strand361-36227
β-strand36518
β-strand37115
α-helix3721
β-strand37811
β-strand38118
β-strand385-38627
β-strand392-39981
β-strand403-41081

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
3-oxoacyl-[acyl-carrier-protein] synthase 2Aprotein427Escherichia coliP0AAI5 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3G11_1 3-oxoacyl-[acyl-carrier-protein] synthase 2 (chains A)
MRGSHHHHHHGSACVSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAY
ATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIG
SGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATAQTS
GVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKE
RDGFVLGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMAN
ALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTIFGEAASRVLVSSTKSMTGHLLGAA
GAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTLCNSFGFGGTNG
SLIFKKI

Ligands and cofactors

IDNameFormulaCopies
P9C3-({3-[(1S,4S,4aS,6S,7S,9S,9aR)-1,6-dimethyl-2-oxo-4-phenyldecahydro-6,9-epoxy-…C30 H33 N O71

Primary citation

Synthesis and biological evaluation of platensimycin analogs. Shen, H.C., Ding, F.X., Singh, S.B. et al. Bioorg Med Chem Lett (2009) 19:1623-1627. DOI 10.1016/j.bmcl.2009.02.006 · PubMed

Other PDB entries of the same protein (UniProt P0AAI5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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