Research workbench
Crystal structure of escherichia COLI phosphoheptose isomerase
Analyse Crystal structure of escherichia COLI phosphoheptose isomerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2I2W
- Type
- protein
- Length
- 739 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoheptose isomerase
- EC
- 5.3.1.-
- UniProt
- P63224
- Pockets
- 6 · best druggability 0.77
Structure
x-ray diffraction · 3 distinct chains · 58% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Phosphoheptose isomerase (EC 5.3.1.-) | protein | 192 | 57% helix, 13% strand | P63224 |
| B | Phosphoheptose isomerase (EC 5.3.1.-) | protein | 177 | 59% helix, 14% strand | P63224 |
| D | Phosphoheptose isomerase (EC 5.3.1.-) | protein | 178 | 57% helix, 13% strand | P63224 |
Ligands and binding sites
- GOL · Glycerol · additive · chains D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1124 | 0.77 | 0.79 | 101 | empty |
| 2 | 132 | 0.55 | 0.82 | 31 | empty |
| 3 | 105 | 0.50 | 0.81 | 27 | empty |
| 4 | 50 | 0.40 | 0.82 | 16 | empty |
| 5 | 90 | 0.38 | 0.76 | 24 | empty |
Interfaces
5 interfaces between chains.
- A–D · 1895 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 1880 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 956 Ų buried · 27 hydrogen bonds · protein-protein
- A–B · 919 Ų buried · 28 hydrogen bonds · protein-protein
- A–C · 231 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P63224
- Elsewhere: RCSB PDB 2I2W · PDBe 2I2W · UniProt P63224
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