Research workbench
Solution structure of the human wild type FAPP1-pH domain
Analyse Solution structure of the human wild type FAPP1-pH domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MDX
- Type
- protein
- Length
- 108 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pleckstrin homology domain-containing family a member 3
- UniProt
- Q9HB20
Structure
solution nmr · 1 distinct chain · 16% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pleckstrin homology domain-containing family a member 3 | protein | 108 | 16% helix, 32% strand | Q9HB20 |
Compared structures
- 2MDX · Solution structure of the human wild type FAPP1-PH domain · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HB20 · AlphaFold monomer V2.0 prediction for pleckstrin homology domain- containing family a… · a predicted model of the same protein · chain A against A, TM-score 0.76
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 Q9HB20
- Elsewhere: RCSB PDB 2MDX · PDBe 2MDX · UniProt Q9HB20
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