Research workbench
Crystal structure of the cytidine deaminase from bacillus anthracis
Analyse Crystal structure of the cytidine deaminase from bacillus anthracis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3B8F
- Type
- protein
- Length
- 565 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative blasticidin S deaminase
- EC
- 3.5.4.4
- UniProt
- Q81Y61
- Pockets
- 6 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 40% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative blasticidin S deaminase (EC 3.5.4.4) | protein | 141 | 40% helix, 21% strand | Q81Y61 |
| B, D | Putative blasticidin S deaminase (EC 3.5.4.4) | protein | 142 | 39% helix, 20% strand | Q81Y61 |
| C | Putative blasticidin S deaminase (EC 3.5.4.4) | protein | 140 | 40% helix, 21% strand | Q81Y61 |
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 168 | 0.82 | 0.97 | 28 | empty |
| 2 | 251 | 0.64 | 0.81 | 25 | empty |
| 3 | 230 | 0.61 | 0.81 | 24 | empty |
| 4 | 208 | 0.59 | 0.80 | 19 | empty |
| 5 | 212 | 0.57 | 0.79 | 25 | empty |
Interfaces
6 interfaces between chains.
- A–D · 1340 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 1339 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1098 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 996 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 297 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3B8F · Crystal structure of the cytidine deaminase from Bacillus anthracis · the same entry in another collection · 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 Q81Y61
- Elsewhere: RCSB PDB 3B8F · PDBe 3B8F · UniProt Q81Y61
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