Research workbench
Water-mediated SUBSTRATE(SLASH)PRODUCT discrimination: the product complex of thymidylate synthase at 1.83 ångströms
Analyse Water-mediated SUBSTRATE(SLASH)PRODUCT discrimination: the product complex of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TYS
- Type
- protein
- Length
- 264 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thymidylate synthase
- EC
- 2.1.1.45
- UniProt
- P00470
- Ligands
- TMP, DHF
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thymidylate synthase (EC 2.1.1.45) | protein | 264 | 37% helix, 26% strand | P00470 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 475 | 0.74 | 0.83 | 47 | TMP, DHF |
| 2 | 61 | 0.27 | 0.73 | 16 | empty |
Modifications
Observed in the structure: 1 modified (carboxylation).
Compared structures
- 1TYS · Water-mediated SUBSTRATE(SLASH)PRODUCT discrimination: the product complex of thymidylate… · the same entry in another collection · chain A against A, TM-score 1.00
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 P00470
- Elsewhere: RCSB PDB 1TYS · PDBe 1TYS · UniProt P00470
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