MolNFT v1 · #88834 · protein
1.57 a crystal structure of erwinia amylovora tyrosine phosphatase amsi
4D74 · Protein-tyrosine-phosphatase amsi: “1.57 a crystal structure of erwinia amylovora tyrosine phosphatase amsi”. X-ray diffraction, 1 ligand (SO4). MolNFT v1 #88834 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4D74
- Type
- protein
- Length
- 151 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein-tyrosine-phosphatase amsi
- EC
- 3.1.3.48
- UniProt
- Q46630
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-tyrosine-phosphatase amsi (EC 3.1.3.48) | protein | 151 | 43% helix, 17% strand | Q46630 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4D74 · 1.57 A crystal structure of erwinia amylovora tyrosine phosphatase amsI · the same entry in another collection · chain A against A, TM-score 1.00
- Q46630 · AlphaFold monomer V2.0 prediction for probable low molecular weight… · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q46630
- Elsewhere: RCSB PDB 4D74 · PDBe 4D74 · UniProt Q46630
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