MolNFT v1 · #17444 · protein
Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase
1OTP: “Structural and theoretical studies suggest domain movement produces an active conformation of thymidine…”. X-ray diffraction, 2 pockets (best druggability 0.75). MolNFT v1 #17444 on GenesisL1: 3D structure, binding sites and pockets…
- 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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