Research workbench
Structure of rabbit muscle phosphoglucomutase at 2.4 ångströms resolution. use of freezing point depressant and reduced temperature to enhance diffractivity
Analyse Structure of rabbit muscle phosphoglucomutase at 2.4 ångströms resolution. use… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PMG
- Type
- protein
- Length
- 1,122 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoglucomutase-1
- EC
- 5.4.2.2
- UniProt
- P00949
- Ligands
- MG
- Pockets
- 13 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phosphoglucomutase-1 (EC 5.4.2.2) | protein | 561 | 36% helix, 25% strand | P00949 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 523 | 0.66 | 0.78 | 55 | empty |
| 2 | 469 | 0.65 | 0.78 | 46 | empty |
| 3 | 374 | 0.61 | 0.77 | 29 | empty |
| 4 | 194 | 0.51 | 0.77 | 26 | empty |
| 5 | 190 | 0.49 | 0.76 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 570 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
Compared structures
- 3PMG · Structure of rabbit muscle phosphoglucomutase at 2.4 ångströms resolution. use of… · the same entry in another collection · chain A against A, TM-score 1.00
- P00949 · AlphaFold monomer V2.0 prediction for phosphoglucomutase-1 (P00949) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P00949
- Elsewhere: RCSB PDB 3PMG · PDBe 3PMG · UniProt P00949
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.