Research workbench
Phosphoglucomutase vanadate based transition state analog complex
Analyse Phosphoglucomutase vanadate based transition state analog complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1C4G
- Type
- protein
- Length
- 1,122 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (alpha-D-glucose 1-phosphate phosphoglucomutase)
- EC
- 2.7.5.1
- UniProt
- P00949
- Ligands
- VG1, CO
- Pockets
- 15 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (alpha-D-glucose 1-phosphate phosphoglucomutase) (EC 2.7.5.1) | protein | 561 | 33% helix, 18% strand | P00949 |
Ligands and binding sites
- VG1 · Alpha-D-glucose-1-phosphate-6-vanadate · ligand · chains A
- CO · Cobalt (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 864 | 0.74 | 0.78 | 68 | VG1 |
| 2 | 702 | 0.70 | 0.78 | 69 | empty |
| 3 | 196 | 0.69 | 0.86 | 28 | empty |
| 4 | 546 | 0.65 | 0.76 | 50 | empty |
| 5 | 390 | 0.65 | 0.78 | 41 | empty |
Interfaces
1 interface between chains.
- A–B · 620 Ų buried · 4 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 P00949
- Elsewhere: RCSB PDB 1C4G · PDBe 1C4G · UniProt P00949
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