Research workbench
Crystal structure of human PRS1 D52H mutant
Analyse Crystal structure of human PRS1 D52H mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F8E
- Type
- protein
- Length
- 616 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribose-phosphate pyrophosphokinase 1
- EC
- 2.7.6.1
- UniProt
- P60891
- Ligands
- MG, SO4
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribose-phosphate pyrophosphokinase 1 (EC 2.7.6.1) | protein | 308 | 37% helix, 24% strand | P60891 |
| B | Ribose-phosphate pyrophosphokinase 1 (EC 2.7.6.1) | protein | 308 | 35% helix, 26% strand | P60891 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1004 | 0.75 | 0.78 | 94 | SO4 |
| 2 | 206 | 0.60 | 0.81 | 29 | empty |
| 3 | 153 | 0.57 | 0.82 | 30 | empty |
| 4 | 79 | 0.38 | 0.78 | 16 | SO4 |
| 5 | 55 | 0.32 | 0.77 | 16 | SO4 |
Interfaces
1 interface between chains.
- A–B · 1486 Ų buried · 20 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 P60891
- Elsewhere: RCSB PDB 4F8E · PDBe 4F8E · UniProt P60891
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