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Crystal structures of human PGM1 isoform 2
Analyse Crystal structures of human PGM1 isoform 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SNP
- Type
- protein
- Length
- 568 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoglucomutase-1
- EC
- 5.4.2.2
- UniProt
- P36871
- Ligands
- MG
- Pockets
- 5 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoglucomutase-1 (EC 5.4.2.2) | protein | 568 | 38% helix, 25% strand | P36871 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 608 | 0.70 | 0.79 | 60 | empty |
| 2 | 124 | 0.41 | 0.75 | 25 | empty |
| 3 | 100 | 0.37 | 0.75 | 23 | empty |
| 4 | 58 | 0.29 | 0.74 | 17 | empty |
| 5 | 53 | 0.25 | 0.73 | 13 | empty |
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 P36871
- Elsewhere: RCSB PDB 6SNP · PDBe 6SNP · UniProt P36871
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