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The crystal structure of yeast cytosine deaminase bound to 4(R)-hydroxyl-3,4-dihydropyrimidine at 1.14 ångströms.
Analyse The crystal structure of yeast cytosine deaminase bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1P6O
- Type
- protein
- Length
- 317 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytosine deaminase
- EC
- 3.5.4.1
- UniProt
- Q12178
- Ligands
- HPY, ZN, CA
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytosine deaminase (EC 3.5.4.1) | protein | 156 | 46% helix, 19% strand | Q12178 |
| B | Cytosine deaminase (EC 3.5.4.1) | protein | 161 | 44% helix, 18% strand | Q12178 |
Ligands and binding sites
- HPY · 4-hydroxy-3,4-dihydro-1H-pyrimidin-2-one · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains B, A
- ACY · Acetic acid · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1559 Ų buried · 28 hydrogen bonds · protein-protein
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 Q12178
- Elsewhere: RCSB PDB 1P6O · PDBe 1P6O · UniProt Q12178
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