Research workbench
Crystal structure of galactose mutarotase galm from bacillus subtilis in complex with maltose and trehalose
Analyse Crystal structure of galactose mutarotase galm from bacillus subtilis in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BZH
- Type
- protein
- Length
- 645 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aldose 1-epimerase
- EC
- 5.1.3.3
- UniProt
- P39840
- Ligands
- GLC
- Pockets
- 4 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aldose 1-epimerase (EC 5.1.3.3) | protein | 322 | 11% helix, 50% strand | P39840 |
| B | Aldose 1-epimerase (EC 5.1.3.3) | protein | 323 | 11% helix, 48% strand | P39840 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 8 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A
- CIT · Citric acid · additive · chains 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 168 | 0.46 | 0.76 | 26 | empty |
| 2 | 92 | 0.39 | 0.76 | 17 | GLC |
| 3 | 103 | 0.38 | 0.75 | 18 | GLC |
| 4 | 59 | 0.32 | 0.76 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 579 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 4BZH · Crystal structure of galactose mutarotase GalM from Bacillus subtilis in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P39840 · AlphaFold monomer V2.0 prediction for aldose 1-epimerase (P39840) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P39840
- Elsewhere: RCSB PDB 4BZH · PDBe 4BZH · UniProt P39840
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.