Research workbench
Domain shifting confirms monomeric structure of escherichia sugar phosphatase suph
Analyse Domain shifting confirms monomeric structure of escherichia sugar phosphatase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HF2
- Type
- protein
- Length
- 536 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sugar phosphatase suph
- EC
- 3.1.3.23
- UniProt
- P75792
- Pockets
- 8 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sugar phosphatase suph (EC 3.1.3.23) | protein | 266 | 37% helix, 23% strand | P75792 |
| B | Sugar phosphatase suph (EC 3.1.3.23) | protein | 270 | 36% helix, 23% strand | P75792 |
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 685 | 0.66 | 0.75 | 63 | empty |
| 2 | 82 | 0.66 | 0.92 | 17 | empty |
| 3 | 72 | 0.62 | 0.90 | 16 | empty |
| 4 | 385 | 0.61 | 0.77 | 48 | empty |
| 5 | 244 | 0.51 | 0.75 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 731 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 modified (engineered).
Compared structures
- 2HF2 · Domain shifting confirms monomeric structure of Escherichia sugar phosphatase SUPH · the same entry in another collection · chain A against A, TM-score 1.00
- P75792 · AlphaFold monomer V2.0 prediction for sugar phosphatase ybiv (P75792) · a predicted model of the same protein · chain B against A, TM-score 0.82
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 P75792
- Elsewhere: RCSB PDB 2HF2 · PDBe 2HF2 · UniProt P75792
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