Research workbench
Crystal structure of his-tag human thymidylate synthase (ht-hts) in complex with fdump
Analyse Crystal structure of his-tag human thymidylate synthase (ht-hts) in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6QXG
- Type
- protein
- Length
- 859 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thymidylate synthase
- EC
- 2.1.1.45
- UniProt
- P04818
- Ligands
- UFP, SO4
- Pockets
- 7 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Thymidylate synthase (EC 2.1.1.45) | protein | 287 | 35% helix, 23% strand | P04818 |
| B | Thymidylate synthase (EC 2.1.1.45) | protein | 285 | 33% helix, 23% strand | P04818 |
Ligands and binding sites
- UFP · 5-fluoro-2'-deoxyuridine-5'-monophosphate · ligand · 3 copies · chains A, B, C
- SO4 · Sulfate ion · ion · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 846 | 0.82 | 0.84 | 103 | UFP, SO4 |
| 2 | 641 | 0.76 | 0.82 | 54 | UFP |
| 3 | 106 | 0.44 | 0.78 | 20 | empty |
| 4 | 134 | 0.40 | 0.74 | 22 | empty |
| 5 | 70 | 0.37 | 0.78 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2221 Ų buried · 32 hydrogen bonds · protein-protein
- B–C · 250 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 215 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6QXG · Crystal structure of His-tag human thymidylate synthase (HT-hTS) in complex with FdUMP · 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 P04818
- Elsewhere: RCSB PDB 6QXG · PDBe 6QXG · UniProt P04818
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