Research workbench
Crystal structure of a human low molecular weight phosphotyrosyl phosphatase. implications for substrate specificity
Analyse Crystal structure of a human low molecular weight phosphotyrosyl phosphatase.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5PNT
- Type
- protein
- Length
- 157 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Low molecular weight phosphotyrosyl phosphatase
- EC
- 3.1.3.2
- UniProt
- P24666
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Low molecular weight phosphotyrosyl phosphatase (EC 3.1.3.2) | protein | 157 | 42% helix, 15% strand | P24666 |
Ligands and binding sites
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5PNT · Crystal structure of a human low molecular weight phosphotyrosyl phosphatase.… · the same entry in another collection · chain A against A, TM-score 1.00
- P24666 · AlphaFold monomer V2.0 prediction for low molecular weight phosphotyrosine protein… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P24666
- Elsewhere: RCSB PDB 5PNT · PDBe 5PNT · UniProt P24666
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