Research workbench
Identification of function and mechanistic insights of guanine deaminase from nitrosomonas europaea: role of the C-terminal loop in catalysis
Analyse Identification of function and mechanistic insights of guanine deaminase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HRQ
- Type
- protein
- Length
- 378 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytidine and deoxycytidylate deaminase zinc-binding region
- UniProt
- Q82Y41
- Ligands
- AZG, ZN
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cytidine and deoxycytidylate deaminase zinc-binding region | protein | 189 | 41% helix, 18% strand | Q82Y41 |
Ligands and binding sites
- AZG · 5-amino-1H-[1,2,3]triazolo[4,5-d]pyrimidin-7-ol · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 212 | 0.55 | 0.78 | 32 | AZG |
| 2 | 69 | 0.31 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1897 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4HRQ · Identification of Function and Mechanistic Insights of Guanine Deaminase from… · 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 Q82Y41
- Elsewhere: RCSB PDB 4HRQ · PDBe 4HRQ · UniProt Q82Y41
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