MolNFT v1 · #75311 · protein
Structure of rabbit muscle phosphoglucomutase at 2.4 ångströms resolution. use of freezing point depressant and reduced temperature to enhance diffractivity
3PMG · Phosphoglucomutase-1: “Structure of rabbit muscle phosphoglucomutase at 2.4 ångströms resolution. use of freezing point depressant…”. X-ray diffraction, 1 ligand (MG), 13 pockets (best druggability 0.66). MolNFT v1 #75311 on…
- 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
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