MolNFT v1 · #12402 · protein
Crystal structure of exocytosis-sensitive phosphoprotein, PP63/PARAFUSIN (phosphoglucomutse) from paramecium. open form
1KFQ · Phosphoglucomutase 1: “Crystal structure of exocytosis-sensitive phosphoprotein, PP63/PARAFUSIN (phosphoglucomutse) from paramecium.…”. X-ray diffraction, 1 ligand (CA), 8 pockets (best druggability 0.78). MolNFT v1 #12402 on…
- PDB
- 1KFQ
- Type
- protein
- Length
- 1,142 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoglucomutase 1
- EC
- 5.4.2.2
- UniProt
- P47244
- Ligands
- CA
- Pockets
- 8 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phosphoglucomutase 1 (EC 5.4.2.2) | protein | 571 | 36% helix, 23% strand | P47244 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1173 | 0.78 | 0.80 | 125 | empty |
| 2 | 922 | 0.77 | 0.80 | 98 | empty |
| 3 | 249 | 0.53 | 0.76 | 27 | empty |
| 4 | 100 | 0.50 | 0.82 | 19 | empty |
| 5 | 205 | 0.48 | 0.75 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1010 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 1KFQ · Crystal Structure of Exocytosis-Sensitive Phosphoprotein, pp63/parafusin… · the same entry in another collection · chain A against A, TM-score 1.00
- P47244 · AlphaFold monomer V2.0 prediction for phosphoglucomutase-1 (P47244) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P47244
- Elsewhere: RCSB PDB 1KFQ · PDBe 1KFQ · UniProt P47244
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