Research workbench
Crystal structure of galactose mutarotase from lactococcus lactis mutant E304A complexed with galactose
Analyse Crystal structure of galactose mutarotase from lactococcus lactis mutant E304A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NS2
- Type
- protein
- Length
- 685 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Galactose mutarotase
- EC
- 5.1.3.3
- UniProt
- Q9ZB17
- Ligands
- GAL, NI
- Pockets
- 8 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Galactose mutarotase (EC 5.1.3.3) | protein | 339 | 9% helix, 45% strand | Q9ZB17 |
| B | Galactose mutarotase (EC 5.1.3.3) | protein | 346 | 9% helix, 43% strand | Q9ZB17 |
Ligands and binding sites
- GAL · beta-D-galactopyranose · sugar · 2 copies · chains A, B
- NI · Nickel (II) ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 97 | 0.77 | 0.98 | 30 | empty |
| 2 | 160 | 0.66 | 0.86 | 30 | GAL |
| 3 | 172 | 0.62 | 0.83 | 30 | GAL |
| 4 | 177 | 0.47 | 0.76 | 32 | empty |
| 5 | 165 | 0.47 | 0.76 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 1024 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 1NS2 · Crystal structure of galactose mutarotase from Lactococcus lactis mutant E304A complexed… · 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 Q9ZB17
- Elsewhere: RCSB PDB 1NS2 · PDBe 1NS2 · UniProt Q9ZB17
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