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Crystal structure of F173G mutant of human aprt
Analyse Crystal structure of F173G mutant of human aprt in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4X45
- Type
- protein
- Length
- 354 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenine phosphoribosyltransferase
- EC
- 2.4.2.7
- UniProt
- P07741
- Ligands
- AMP
- Pockets
- 2 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenine phosphoribosyltransferase (EC 2.4.2.7) | protein | 179 | 35% helix, 34% strand | P07741 |
| B | Adenine phosphoribosyltransferase (EC 2.4.2.7) | protein | 175 | 36% helix, 31% strand | P07741 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains 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 | 420 | 0.66 | 0.79 | 33 | empty |
| 2 | 209 | 0.50 | 0.76 | 26 | AMP |
Interfaces
1 interface between chains.
- A–B · 1586 Ų buried · 19 hydrogen bonds · protein-protein
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 P07741
- Elsewhere: RCSB PDB 4X45 · PDBe 4X45 · UniProt P07741
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