Research workbench
Crystal structure of the conserved N-terminal domain of the peroxisomal matrix-protein-import receptor, PEX14P
Analyse Crystal structure of the conserved N-terminal domain of the peroxisomal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FF5
- Type
- protein
- Length
- 108 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peroxisomal biogenesis factor 14
- UniProt
- Q642G4
- Ligands
- DPW
Structure
x-ray diffraction · 1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Peroxisomal biogenesis factor 14 | protein | 54 | 72% helix, 0% strand | Q642G4 |
Ligands and binding sites
- DPW · decyl 2-trimethylazaniumylethyl phosphate · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 614 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 3FF5 · Crystal structure of the conserved N-terminal domain of the peroxisomal… · the same entry in another collection · chain A against A, TM-score 1.00
- Q642G4 · AlphaFold monomer V2.0 prediction for peroxisomal membrane protein PEX14 (Q642G4) · a predicted model of the same protein · chain A against A, TM-score 0.88
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 Q642G4
- Elsewhere: RCSB PDB 3FF5 · PDBe 3FF5 · UniProt Q642G4
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