1L0H: Butyryl-ACP from e.coli

Crystal structure of butyryl-ACP from e.coli. Determined by X-ray diffraction at 2.0 Å resolution. Released 11 Feb 2003.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Escherichia coli
Chains
1
Atoms
651
Mol. weight
8.78 kDa
Ligands
ZN
Released
11 Feb 2003

Explore 1L0H in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1L0H contains 5 α-helices and 2 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: 5 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix3-1513
α-helix19-213
β-strand2711
α-helix36-4914
α-helix56-594
β-strand6411
α-helix65-7410

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Acyl carrier proteinAprotein78Escherichia coliP0A6A8 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1L0H_1 ACYL CARRIER PROTEIN (chains A)
MSTIEERVKKIIGEQLGVKQEEVTNNASFVEDLGADSLDTVELVMALEEEFDTEIPDEEA
EKITTVQAAIDYINGHQA

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

Primary citation

X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site. Roujeinikova, A., Baldock, C., Simon, W.J. et al. Structure (2002) 10:825-835. DOI 10.1016/S0969-2126(02)00775-X · PubMed

Other PDB entries of the same protein (UniProt P0A6A8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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