Research workbench
Crystal structure of bacillus subtilis guanine deaminase. the first domain-swapped structure in the cytidine deaminase superfamily
Analyse Crystal structure of bacillus subtilis guanine deaminase. the first… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WKQ
- Type
- protein
- Length
- 313 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanine deaminase
- EC
- 3.5.4.3
- UniProt
- O34598
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanine deaminase (EC 3.5.4.3) | protein | 158 | 44% helix, 18% strand | O34598 |
| B | Guanine deaminase (EC 3.5.4.3) | protein | 155 | 45% helix, 18% strand | O34598 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 3995 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 1WKQ · Crystal Structure of Bacillus subtilis Guanine Deaminase. The first domain-swapped… · the same entry in another collection · chain A against A, TM-score 1.00
- O34598 · AlphaFold monomer V2.0 prediction for guanine deaminase (O34598) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 O34598
- Elsewhere: RCSB PDB 1WKQ · PDBe 1WKQ · UniProt O34598
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