Research workbench
Crystal structure of thymidylate synthase from elizabethkingia anophelis NUHP1
Analyse Crystal structure of thymidylate synthase from elizabethkingia anophelis NUHP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AUJ
- Type
- protein
- Length
- 757 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thymidylate synthase
- EC
- 2.1.1.45
- UniProt
- A0A077EAN3
- Pockets
- 9 · best druggability 0.71
Structure
x-ray diffraction · 3 distinct chains · 38% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thymidylate synthase (EC 2.1.1.45) | protein | 248 | 39% helix, 29% strand | A0A077EAN3 |
| B | Thymidylate synthase (EC 2.1.1.45) | protein | 258 | 36% helix, 28% strand | A0A077EAN3 |
| C | Thymidylate synthase (EC 2.1.1.45) | protein | 251 | 39% helix, 28% strand | A0A077EAN3 |
Ligands and binding sites
- PGE · Triethylene glycol · additive · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 648 | 0.71 | 0.79 | 79 | empty |
| 2 | 367 | 0.63 | 0.78 | 42 | PGE |
| 3 | 290 | 0.59 | 0.78 | 27 | PGE |
| 4 | 199 | 0.56 | 0.79 | 23 | PGE |
| 5 | 155 | 0.47 | 0.76 | 21 | empty |
Interfaces
3 interfaces between chains.
- B–C · 2179 Ų buried · 38 hydrogen bonds · protein-protein
- A–B · 462 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 160 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (nonstandard).
Compared structures
- 6AUJ · Crystal structure of thymidylate synthase from Elizabethkingia anophelis NUHP1 · 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 A0A077EAN3
- Elsewhere: RCSB PDB 6AUJ · PDBe 6AUJ · UniProt A0A077EAN3
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