Research workbench
Crystal structure of putative sugar phosphate isomerase (AFE_0303) from acidithiobacillus ferrooxidans atcc 23270 at 1.85 a resolution
Analyse Crystal structure of putative sugar phosphate isomerase (AFE_0303) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3L2H
- Type
- protein
- Length
- 631 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative sugar phosphate isomerase
- UniProt
- B7J8Z8
- Ligands
- CL
- Pockets
- 5 · best druggability 0.70
Structure
x-ray diffraction · 4 distinct chains · 13% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative sugar phosphate isomerase | protein | 158 | 13% helix, 53% strand | B7J8Z8 |
| B | Putative sugar phosphate isomerase | protein | 159 | 14% helix, 53% strand | B7J8Z8 |
| C | Putative sugar phosphate isomerase | protein | 158 | 13% helix, 53% strand | B7J8Z8 |
| D | Putative sugar phosphate isomerase | protein | 156 | 12% helix, 54% strand | B7J8Z8 |
Ligands and binding sites
- CL · Chloride ion · ion · 3 copies · chains A, D, B
- EDO · 1,2-ethanediol · additive · 14 copies · chains A, D, B, C
- CXS · 3-cyclohexyl-1-propylsulfonic acid · additive · 4 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 440 | 0.70 | 0.81 | 36 | EDO |
| 2 | 503 | 0.70 | 0.80 | 37 | EDO |
| 3 | 476 | 0.70 | 0.80 | 39 | EDO |
| 4 | 525 | 0.70 | 0.79 | 42 | EDO |
| 5 | 387 | 0.53 | 0.72 | 33 | empty |
Interfaces
4 interfaces between chains.
- B–C · 1730 Ų buried · 23 hydrogen bonds · protein-protein
- A–D · 1704 Ų buried · 23 hydrogen bonds · protein-protein
- A–C · 1195 Ų buried · 18 hydrogen bonds · protein-protein
- B–D · 1156 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 19 modified (engineered).
Compared structures
- 3L2H · Crystal structure of Putative sugar phosphate isomerase (AFE_0303) from Acidithiobacillus… · the same entry in another collection · chain A against A, TM-score 1.00
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 B7J8Z8
- Elsewhere: RCSB PDB 3L2H · PDBe 3L2H · UniProt B7J8Z8
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