Research workbench
Crystal structure of the S-nitrosylated CYS215 of PTP1B
Analyse Crystal structure of the S-nitrosylated CYS215 of PTP1B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EU0
- Type
- protein
- Length
- 281 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein phosphatase non-receptor type 1
- EC
- 3.1.3.48
- UniProt
- P18031
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein phosphatase non-receptor type 1 (EC 3.1.3.48) | protein | 281 | 37% helix, 21% strand | P18031 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.37 | 0.75 | 21 | empty |
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 3EU0 · Crystal structure of the S-nitrosylated Cys215 of PTP1B · 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 3EU0 · PDBe 3EU0 · UniProt P18031
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