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Crystal structures of SULT1A2 and SULT1A1*3: implications in the bioactivation of N-hydroxy-2-acetylamino fluorine (oh-aaf)
Analyse Crystal structures of SULT1A2 and SULT1A1*3: implications in the bioactivation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z28
- Type
- protein
- Length
- 289 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P50225
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 289 | — | P50225 |
Compared structures
- 1Z28 · Crystal Structures of SULT1A2 and SULT1A1*3: Implications in the bioactivation of… · the same entry in another collection · chain A against A, TM-score 1.00
- P50225 · AlphaFold monomer V2.0 prediction for sulfotransferase 1A1 (P50225) · 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 P50225
- Elsewhere: RCSB PDB 1Z28 · PDBe 1Z28 · UniProt P50225
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