1T8K: Apo acyl carrier protein from E. coli

Crystal Structure of apo acyl carrier protein from E. coli. Determined by X-ray diffraction at 1.1 Å resolution. Released 7 Sept 2004.

Method
X-ray diffraction
Resolution
1.1 Å
Organism
Escherichia coli
Chains
1
Atoms
750
Mol. weight
9.58 kDa
Ligands
ZN
Released
7 Sept 2004

Explore 1T8K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1T8K 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-helix36-5015
α-helix56-594
β-strand6411
α-helix65-7410

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Acyl carrier proteinAprotein77Escherichia coliP0A6A8 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1T8K_1 Acyl carrier protein (chains A)
STIEERVKKIIGEQLGVKQEEVTNNASFVEDLGADSLDTVELVMALEEEFDTEIPDEEAE
KITTVQAAIDYINGHQA

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn10

Water and common crystallization additives (IMD) are not listed.

Primary citation

Structure of apo acyl carrier protein and a proposal to engineer protein crystallization through metal ions. Qiu, X., Janson, C.A. Acta Crystallogr D Biol Crystallogr (2004) 60:1545-1554. DOI 10.1107/S0907444904015422 · 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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