1LP1: Protein Z

Protein Z in complex with an in vitro selected affibody. Determined by X-ray diffraction at 2.3 Å resolution. Released 18 Mar 2003.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Staphylococcus aureus
Chains
2
Atoms
1,071
Mol. weight
13.5 kDa
Ligands
MG
Released
18 Mar 2003

Explore 1LP1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1LP1 contains 7 α-helices and 0 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: 4 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix5-1713
α-helix24-3613
α-helix38-403
α-helix41-5414
Chain B: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix6-1611
α-helix24-3613
α-helix41-5414

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Affibody binding protein ZAprotein58Staphylococcus aureus
Immunoglobulin G binding protein ABprotein58Staphylococcus aureusP38507 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1LP1_1 Affibody binding protein Z (chains A)
VDNKFNKELSVAGREIVTLPNLNDPQKKAFIFSLWDDPSQSANLLAEAKKLNDAQAPK
Sequence of entity 2 (B), FASTA
>1LP1_2 Immunoglobulin G binding protein A (chains B)
VDNKFNKEQQNAFYEILHLPNLNEEQRNAFIQSLKDDPSQSANLLAEAKKLNDAQAPK

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Structural basis for recognition by an in vitro evolved affibody. Hogbom, M., Eklund, M., Nygren, P.A. et al. Proc Natl Acad Sci U S A (2003) 100:3191-3196. DOI 10.1073/pnas.0436100100 · PubMed

Other PDB entries of the same protein (UniProt P38507 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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