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Crystal structures of D-allulose 3-epimerase with D-allulose from sinorhizobium fredii
Analyse Crystal structures of D-allulose 3-epimerase with D-allulose from sinorhizobium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DZ6
- Type
- protein
- Length
- 1,132 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D-tagatose 3-epimerase
- EC
- 5.1.3.-
- UniProt
- A0A249Q1V1
- Ligands
- PSJ, MG
- Pockets
- 12 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | D-tagatose 3-epimerase (EC 5.1.3.-) | protein | 283 | 46% helix, 15% strand | A0A249Q1V1 |
Ligands and binding sites
- PSJ · D-psicose · ligand · 2 copies · chains C, D
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 587 | 0.87 | 0.93 | 58 | empty |
| 2 | 72 | 0.75 | 0.98 | 22 | PSJ |
| 3 | 72 | 0.74 | 0.98 | 23 | PSJ |
| 4 | 241 | 0.67 | 0.84 | 36 | empty |
| 5 | 258 | 0.66 | 0.83 | 32 | empty |
Interfaces
6 interfaces between chains.
- A–C · 1640 Ų buried · 30 hydrogen bonds · protein-protein
- B–D · 1594 Ų buried · 26 hydrogen bonds · protein-protein
- A–B · 560 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 559 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 406 Ų buried · 7 hydrogen bonds · protein-protein
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 A0A249Q1V1
- Elsewhere: RCSB PDB 7DZ6 · PDBe 7DZ6 · UniProt A0A249Q1V1
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