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
- 1OTP
- Type
- protein
- Length
- 440 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thymidine phosphorylase
- EC
- 2.4.2.4
- UniProt
- P07650
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thymidine phosphorylase (EC 2.4.2.4) | protein | 440 | 46% helix, 15% strand | P07650 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 682 | 0.75 | 0.81 | 56 | empty |
| 2 | 50 | 0.32 | 0.78 | 11 | empty |
Compared structures
- 1OTP · 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 1OTP · PDBe 1OTP · UniProt P07650
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