Research workbench
Crystal structure of the complex formed between the catalytic domain of shp-1 and an in vitro peptide substrate PY469 derived from shps-1.
Analyse Crystal structure of the complex formed between the catalytic domain of shp-1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FPR
- Type
- protein
- Length
- 294 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P29350
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 284 | — | P29350 |
| B | — | protein | 10 | — | — |
Compared structures
- 1FPR · Crystal structure of the complex formed between the catalytic domain of shp-1 and an in… · the same entry in another collection · chain A against A, TM-score 1.00
- P29350 · AlphaFold monomer V2.0 prediction for tyrosine-protein phosphatase non-receptor type 6… · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P29350
- Elsewhere: RCSB PDB 1FPR · PDBe 1FPR · UniProt P29350
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