Research workbench
Crystal structure of human aprt wild type in complex with phosphate ion.
Analyse Crystal structure of human aprt wild type in complex with phosphate ion. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HGP
- Type
- protein
- Length
- 347 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
- PO4
- Pockets
- 4 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenine phosphoribosyltransferase (EC 2.4.2.7) | protein | 175 | 36% helix, 34% strand | P07741 |
| B | Adenine phosphoribosyltransferase (EC 2.4.2.7) | protein | 172 | 37% helix, 33% strand | P07741 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
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 | 320 | 0.60 | 0.78 | 33 | PO4 |
| 2 | 265 | 0.54 | 0.76 | 35 | PO4 |
| 3 | 56 | 0.48 | 0.85 | 13 | empty |
| 4 | 99 | 0.39 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1558 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 6HGP · Crystal Structure of Human APRT wild type in complex with Phosphate ion. · the same entry in another collection · chain A against A, TM-score 1.00
- P07741 · AlphaFold monomer V2.0 prediction for adenine phosphoribosyltransferase (P07741) · a predicted model of the same protein · chain B 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 P07741
- Elsewhere: RCSB PDB 6HGP · PDBe 6HGP · UniProt P07741
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