Research workbench
Crystal structure of thymidylate kinase with tmp and its low- resolution (saxs) solution structure from brugia malayi
Analyse Crystal structure of thymidylate kinase with tmp and its low- resolution (saxs)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7FGQ
- Type
- protein
- Length
- 190 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A1P6BP23
- Ligands
- TMP
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 190 | — | A0A1P6BP23 |
Ligands and binding sites
- TMP · Thymidine-5'-phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7FGQ · Crystal structure of Thymidylate kinase with TMP and its low-resolution (SAXS) solution… · 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 A0A1P6BP23
- Elsewhere: RCSB PDB 7FGQ · PDBe 7FGQ · UniProt A0A1P6BP23
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