Research workbench
Human guanine deaminase in complex with valacyclovir
Analyse Human guanine deaminase in complex with valacyclovir in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AQL
- Type
- protein
- Length
- 442 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanine deaminase
- EC
- 3.5.4.3
- UniProt
- Q9Y2T3
- Ligands
- TXC, ZN
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanine deaminase (EC 3.5.4.3) | protein | 442 | 42% helix, 21% strand | Q9Y2T3 |
Ligands and binding sites
- TXC · 2-[(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)methoxy]ethyl L-valinate · ligand · chains A
- ZN · Zinc ion · metal · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 175 | 0.65 | 0.85 | 30 | TXC |
| 2 | 150 | 0.51 | 0.79 | 23 | empty |
| 3 | 62 | 0.34 | 0.77 | 11 | empty |
| 4 | 61 | 0.34 | 0.77 | 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 Q9Y2T3
- Elsewhere: RCSB PDB 4AQL · PDBe 4AQL · UniProt Q9Y2T3
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