1TEG: Plastocyanin, chloroplast

Crystal structure of the spinach plastocyanin mutants G8D/K30C/T69C and K30C/T69C- a study of the effect on crystal packing and thermostability from the introduction of a novel disulfide bond. Determined by X-ray diffraction at 1.96 Å resolution. Released 1 Nov 2005.

Method
X-ray diffraction
Resolution
1.96 Å
Organism
Spinacia oleracea
Chains
2
Atoms
1,547
Mol. weight
20.96 kDa
Ligands
CU
Released
1 Nov 2005

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

Secondary structure: helices and β-sheets

1TEG contains 5 α-helices and 20 β-strands across 2 chains. 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: 3 helices, 10 β-strands

ElementResiduesLengthSheet
β-strand2-541
β-strand14-1521
β-strand18-2142
β-strand26-3161
β-strand3713
β-strand40-4122
α-helix43-453
α-helix52-554
β-strand6313
β-strand69-7351
β-strand78-8362
α-helix85-906
β-strand93-9862
Chain B: 2 helices, 10 β-strands
ElementResiduesLengthSheet
β-strand2-544
β-strand14-1524
β-strand18-2145
β-strand26-3164
β-strand3716
β-strand40-4125
α-helix52-554
β-strand6316
β-strand69-7354
β-strand78-8365
α-helix85-906
β-strand93-9865

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Plastocyanin, chloroplastA, Bprotein99Spinacia oleraceaP00289 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1TEG_1 Plastocyanin, chloroplast (chains A, B)
VEVLLGGGDGSLAFLPGDFSVASGEEIVFCNNAGFPHNVVFDEDEIPSGVDAAKISMSEE
DLLNAPGECYKVTLTEKGTYKFYCSPHQGAGMVGKVTVN

Ligands and cofactors

IDNameFormulaCopies
CUCopper (II) ionCu2

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

Primary citation

Novel Disulfide Bonds Effect the Thermostability of Plastocyanin. Crystal structures of the triple plastocyanin mutant G8D/K30C/T69C and the double plastocyanin mutant K30C/T69C from spinach at 1.90 A and 1.96 A resolution, respectively. Okvist, M., Jacobson, F., Jansson, H. et al. To be published.

Other PDB entries of the same protein (UniProt P00289 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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