MolNFT v1 · #64568 · protein
Bacterial cytosine deaminase V152A/F316C/D317G mutant
3G77: “Bacterial cytosine deaminase V152A/F316C/D317G mutant”. X-ray diffraction, 1 ligand (FE), 1 pocket (best druggability 0.32). MolNFT v1 #64568 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3G77
- 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
- FE
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytosine deaminase (EC 3.5.4.1) | protein | 423 | 37% helix, 22% strand | P25524 |
Ligands and binding sites
- FE · Fe (III) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 62 | 0.32 | 0.76 | 13 | 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 3G77 · PDBe 3G77 · UniProt P25524
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