Research workbench
Rabbit muscle phosphoglucomutase
Analyse Rabbit muscle phosphoglucomutase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VKL
- Type
- protein
- Length
- 1,122 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoglucomutase
- EC
- 5.4.2.2
- UniProt
- P00949
- Ligands
- NI
- Pockets
- 14 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phosphoglucomutase (EC 5.4.2.2) | protein | 561 | 36% helix, 26% strand | P00949 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 588 | 0.69 | 0.79 | 58 | empty |
| 2 | 433 | 0.63 | 0.78 | 38 | empty |
| 3 | 328 | 0.63 | 0.79 | 31 | empty |
| 4 | 188 | 0.52 | 0.78 | 25 | empty |
| 5 | 187 | 0.49 | 0.76 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 599 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
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 P00949
- Elsewhere: RCSB PDB 1VKL · PDBe 1VKL · UniProt P00949
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