Research workbench
NMR structure in a membrane environment reveals putative amyloidogenic regions of the sevi precursor peptide PAP248-286
Analyse NMR structure in a membrane environment reveals putative amyloidogenic regions… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2L3H
- Type
- protein
- Length
- 39 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prostatic acid phosphatase
- EC
- 3.1.3.2
- UniProt
- P15309
Structure
solution nmr · 1 distinct chain · 26% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prostatic acid phosphatase (EC 3.1.3.2) | protein | 39 | 26% helix, 0% strand | P15309 |
Compared structures
- 2L3H · NMR Structure in a Membrane Environment Reveals Putative Amyloidogenic Regions of the… · the same entry in another collection · chain A against A, TM-score 1.00
- P15309 · AlphaFold monomer V2.0 prediction for prostatic acid phosphatase (P15309) · a predicted model of the same protein · chain A against A, TM-score 0.34
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P15309
- Elsewhere: RCSB PDB 2L3H · PDBe 2L3H · UniProt P15309
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