Research workbench
Crystal structure of apo human PTP1B (C215S) mutant
Analyse Crystal structure of apo human PTP1B (C215S) mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1I57
- Type
- protein
- Length
- 284 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phospho-tyrosine phosphatase 1B
- EC
- 3.1.3.48
- UniProt
- P18031
- Ligands
- MG, CL
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospho-tyrosine phosphatase 1B (EC 3.1.3.48) | protein | 284 | 36% helix, 23% strand | P18031 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 112 | 0.48 | 0.80 | 29 | CL |
| 2 | 56 | 0.29 | 0.75 | 16 | empty |
Compared structures
- 1I57 · Crystal structure of apo human PTP1B (C215S) mutant · 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 1I57 · PDBe 1I57 · UniProt P18031
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