Research workbench
Bacterial cytosine deaminase D314S mutant.
Analyse Bacterial cytosine deaminase D314S mutant. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1R9Z
- Type
- protein
- Length
- 423 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytosine deaminase
- UniProt
- P25524
- Ligands
- FE, MG
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytosine deaminase | protein | 423 | 37% helix, 23% strand | P25524 |
Ligands and binding sites
- FE · Fe (III) ion · metal · chains A
- MG · Magnesium 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
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 384 | 0.68 | 0.80 | 41 | MG |
| 2 | 80 | 0.36 | 0.76 | 20 | empty |
| 3 | 50 | 0.31 | 0.77 | 12 | empty |
| 4 | 59 | 0.24 | 0.72 | 18 | 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 1R9Z · PDBe 1R9Z · UniProt P25524
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