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Crystal structure of the S62A mutant of phosphoglycerate mutase from bacillus stearothermophilus complexed with 2-phosphoglycerate
Analyse Crystal structure of the S62A mutant of phosphoglycerate mutase from bacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1O99
- Type
- protein
- Length
- 509 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- EC
- 5.4.2.1
- UniProt
- Q9X519
- Ligands
- 2PG, MN, SO4
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (EC 5.4.2.1) | protein | 509 | 38% helix, 17% strand | Q9X519 |
Ligands and binding sites
- 2PG · 2-phosphoglyceric acid · ligand · chains A
- MN · Manganese (II) ion · metal · chains A
- SO4 · Sulfate ion · ion · 6 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 255 | 0.67 | 0.84 | 36 | empty |
| 2 | 241 | 0.67 | 0.84 | 36 | empty |
| 3 | 240 | 0.58 | 0.79 | 28 | SO4 |
| 4 | 56 | 0.29 | 0.74 | 13 | empty |
Compared structures
- 1O99 · Crystal structure of the S62A mutant of phosphoglycerate mutase from bacillus… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9X519 · AlphaFold monomer V2.0 prediction for 2,3-bisphosphoglycerate- independent… · a predicted model of the same protein · chain A against A, TM-score 0.66
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 Q9X519
- Elsewhere: RCSB PDB 1O99 · PDBe 1O99 · UniProt Q9X519
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