Research workbench
Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase
Analyse Structural and theoretical studies suggest domain movement produces an active… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AZY
- Type
- protein
- Length
- 880 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P07650
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 440 | — | P07650 |
Compared structures
- 1AZY · Structural and theoretical studies suggest domain movement produces an active… · the same entry in another collection · chain A against A, TM-score 1.00
- P07650 · AlphaFold monomer V2.0 prediction for thymidine phosphorylase (P07650) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P07650
- Elsewhere: RCSB PDB 1AZY · PDBe 1AZY · UniProt P07650
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.