Research workbench
Crystal structure of the PTS1 complexed to the tpr region of human PEX5
Analyse Crystal structure of the PTS1 complexed to the tpr region of human PEX5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FCH
- Type
- protein
- Length
- 609 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P50542
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 302 | — | P50542 |
| B | — | protein | 297 | — | P50542 |
| C, D | — | protein | 5 | — | — |
Compared structures
- 1FCH · Crystal structure of the PTS1 complexed to the tpr region of human PEX5 · the same entry in another collection · chain A against A, TM-score 1.00
- P50542 · AlphaFold monomer V2.0 prediction for peroxisomal targeting signal 1 receptor (P50542) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P50542
- Elsewhere: RCSB PDB 1FCH · PDBe 1FCH · UniProt P50542
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