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Crystal structure of the 4TH FN3 domain of human protein tyrosine phosphatase, receptor type F [psi-nysgrc-006240]
Analyse Crystal structure of the 4TH FN3 domain of human protein tyrosine phosphatase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4N5U
- Type
- protein
- Length
- 108 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-type tyrosine-protein phosphatase F
- EC
- 3.1.3.48
- UniProt
- P10586
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Receptor-type tyrosine-protein phosphatase F (EC 3.1.3.48) | protein | 108 | 3% helix, 51% strand | P10586 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4N5U · Crystal structure of the 4th FN3 domain of human Protein Tyrosine phosphatase, receptor… · the same entry in another collection · chain A against A, TM-score 1.00
- P10586 · AlphaFold monomer V2.0 prediction for receptor-type tyrosine-protein phosphatase F… · 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 P10586
- Elsewhere: RCSB PDB 4N5U · PDBe 4N5U · UniProt P10586
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