Research workbench
PTP1B R47C modified at C47 with N-[4-(2-{2-[3-(2-bromo-acetylamino)- propionylamino]-3-hydroxy-propionylamino}-ethyl)-phenyl]-oxalamic acid
Analyse PTP1B R47C modified at C47 with N-[4-(2-{2-[3-(2-bromo-acetylamino)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NWE
- Type
- protein
- Length
- 296 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein-tyrosine phosphatase, non-receptor type 1
- EC
- 3.1.3.48
- UniProt
- P18031
- Ligands
- FG1
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-tyrosine phosphatase, non-receptor type 1 (EC 3.1.3.48) | protein | 296 | 36% helix, 23% strand | P18031 |
Ligands and binding sites
- FG1 · N-[4-(2-{2-[3-(2-bromo-acetylamino)-propionylamino]-3-hydroxy-propionylamino}-ethyl)-phenyl]-oxalamic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1NWE · Ptp1B R47C Modified at C47 with N-[4-(2-{2-[3-(2-Bromo-acetylamino)-propionylamino]-3-hydr… · the same entry in another collection · chain A against A, TM-score 1.00
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 P18031
- Elsewhere: RCSB PDB 1NWE · PDBe 1NWE · UniProt P18031
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