2FS1: PSD-1

solution structure of PSD-1. Determined by solution NMR. Released 5 Dec 2006.

Method
Solution NMR
Organisms
Finegoldia magna ATCC 29328, Streptococcus dysgalactiae, Streptococcus equi
Chains
1
Atoms
431
Mol. weight
6.15 kDa
Released
5 Dec 2006

Explore 2FS1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2FS1 contains 3 α-helices and 0 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: 3 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix5-2319
α-helix27-348
α-helix40-5112

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
PSD-1Aprotein56Finegoldia magna ATCC 29328, Streptococcus dysgalactiae, Streptococcus equi, Streptococcus canis, Streptococcus sp.Q51918 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2FS1_1 PSD-1 (chains A)
MEAVDANSLAQAKEAAIKELKQYGIGDYYIKLINNAKTVEGVESLKNEILKALPTE

Primary citation

Structure, dynamics, and stability variation in bacterial albumin binding modules: implications for species specificity. He, Y., Rozak, D.A., Sari, N. et al. Biochemistry (2006) 45:10102-10109. DOI 10.1021/bi060409m · PubMed

Other PDB entries of the same protein (UniProt Q51918 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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