Research workbench
Crystal structure of cytosine deaminase from escherichia COLI complexed with zinc and isoguanine
Analyse Crystal structure of cytosine deaminase from escherichia COLI complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RN6
- Type
- protein
- Length
- 422 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
- PXN, IGA, ZN
- Pockets
- 3 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytosine deaminase (EC 3.5.4.1) | protein | 422 | 36% helix, 23% strand | P25524 |
Ligands and binding sites
- PXN · (2S)-1-[3-{[(2R)-2-hydroxypropyl]oxy}-2,2-bis({[(2R)-2-hydroxypropyl]oxy}methyl)propoxy]propan-2-ol · ligand · chains A
- IGA · 6-amino-3,7-dihydro-2H-purin-2-one · ligand · chains A
- ZN · Zinc ion · metal · 2 copies · 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 | 87 | 0.37 | 0.76 | 23 | empty |
| 2 | 94 | 0.34 | 0.74 | 22 | empty |
| 3 | 76 | 0.34 | 0.76 | 13 | empty |
Compared structures
- 3RN6 · Crystal structure of Cytosine Deaminase from Escherichia Coli complexed with zinc and… · the same entry in another collection · chain A against A, TM-score 1.00
- P25524 · AlphaFold monomer V2.0 prediction for cytosine deaminase (P25524) · a predicted model of the same protein · 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 P25524
- Elsewhere: RCSB PDB 3RN6 · PDBe 3RN6 · UniProt P25524
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