MolNFT v1 · #21206 · protein
Crystal structure of the D58A phosphoenolpyruvate mutase mutant protein
1S2U · Phosphoenolpyruvate phosphomutase: “Crystal structure of the D58A phosphoenolpyruvate mutase mutant protein”. X-ray diffraction, 4 pockets (best druggability 0.60). MolNFT v1 #21206 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1S2U
- Type
- protein
- Length
- 579 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoenolpyruvate phosphomutase
- EC
- 5.4.2.9
- UniProt
- P56839
- Pockets
- 4 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoenolpyruvate phosphomutase (EC 5.4.2.9) | protein | 290 | 47% helix, 13% strand | P56839 |
| B | Phosphoenolpyruvate phosphomutase (EC 5.4.2.9) | protein | 289 | 47% helix, 13% strand | P56839 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 341 | 0.60 | 0.77 | 41 | PEG |
| 2 | 566 | 0.59 | 0.73 | 59 | empty |
| 3 | 306 | 0.57 | 0.77 | 40 | PEG |
| 4 | 113 | 0.55 | 0.83 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1150 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 1S2U · Crystal structure of the D58A phosphoenolpyruvate mutase mutant protein · the same entry in another collection · chain A against A, TM-score 1.00
- P56839 · AlphaFold monomer V2.0 prediction for phosphoenolpyruvate phosphomutase (P56839) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 P56839
- Elsewhere: RCSB PDB 1S2U · PDBe 1S2U · UniProt P56839
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