Research workbench
Human thymidylate synthase complexed with dcmp
Analyse Human thymidylate synthase complexed with dcmp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WRN
- Type
- protein
- Length
- 1,697 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04818
- Ligands
- DC
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 282 | — | P04818 |
| A | — | protein | 284 | — | P04818 |
| C | — | protein | 282 | — | P04818 |
| D, E | — | protein | 286 | — | P04818 |
| F | — | protein | 277 | — | P04818 |
Ligands and binding sites
- DC · 2'-deoxycytidine-5'-monophosphate · ligand · 6 copies · chains B, A, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5WRN · Human thymidylate synthase complexed with dCMP · the same entry in another collection · chain B against B, 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 5WRN · PDBe 5WRN · UniProt P04818
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