MolNFT v1 · #135171 · protein
Crystal structure of the D263G missense variant of human PGM1
5TR2 · Phosphoglucomutase-1: “Crystal structure of the D263G missense variant of human PGM1”. X-ray diffraction, 2 ligands (CA, SO4), 12 pockets (best druggability 0.72). MolNFT v1 #135171 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5TR2
- Type
- protein
- Length
- 1,113 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoglucomutase-1
- EC
- 5.4.2.2
- UniProt
- P36871
- Ligands
- CA, SO4
- Pockets
- 12 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoglucomutase-1 (EC 5.4.2.2) | protein | 561 | 36% helix, 25% strand | P36871 |
| B | Phosphoglucomutase-1 (EC 5.4.2.2) | protein | 552 | 36% helix, 24% strand | P36871 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 723 | 0.72 | 0.78 | 73 | SO4, GOL |
| 2 | 500 | 0.65 | 0.78 | 60 | SO4 |
| 3 | 64 | 0.63 | 0.91 | 22 | empty |
| 4 | 348 | 0.58 | 0.76 | 46 | empty |
| 5 | 122 | 0.57 | 0.84 | 33 | empty |
Interfaces
1 interface between chains.
- A–B · 141 Ų buried · 1 hydrogen bond · 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 P36871
- Elsewhere: RCSB PDB 5TR2 · PDBe 5TR2 · UniProt P36871
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