2L3H: Prostatic acid phosphatase

NMR Structure in a Membrane Environment Reveals Putative Amyloidogenic Regions of the SEVI Precursor Peptide PAP248-286. Determined by solution NMR. Released 6 Oct 2010.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
319
Mol. weight
4.56 kDa
Released
6 Oct 2010

Explore 2L3H in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2L3H contains 2 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: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix262-2687
α-helix282-2843

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Prostatic acid phosphataseAprotein39Homo sapiensP15309 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2L3H_1 Prostatic acid phosphatase (chains A)
GIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMY

Primary citation

NMR structure in a membrane environment reveals putative amyloidogenic regions of the SEVI precursor peptide PAP(248-286). Nanga, R.P., Brender, J.R., Vivekanandan, S. et al. J Am Chem Soc (2009) 131:17972-17979. DOI 10.1021/ja908170s · PubMed

Other PDB entries of the same protein (UniProt P15309 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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