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Bacterial cytosine deaminase D314S mutant bound to 5-fluoro-4-(S)- hydroxyl-3,4-dihydropyrimidine.
Analyse Bacterial cytosine deaminase D314S mutant bound to 5-fluoro-4-(S)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RAK
- Type
- protein
- Length
- 423 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytosine deaminase
- EC
- 3.5.4.1
- UniProt
- P25524
- Ligands
- FPY, FE
- Pockets
- 3 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytosine deaminase (EC 3.5.4.1) | protein | 423 | 37% helix, 23% strand | P25524 |
Ligands and binding sites
- FPY · (4S)-5-fluoro-4-hydroxy-3,4-dihydropyrimidin-2(1H)-one · ligand · chains A
- FE · Fe (III) ion · metal · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.33 | 0.75 | 22 | empty |
| 2 | 51 | 0.24 | 0.72 | 16 | empty |
| 3 | 50 | 0.23 | 0.72 | 11 | empty |
Compared structures
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 P25524
- Elsewhere: RCSB PDB 1RAK · PDBe 1RAK · UniProt P25524
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