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Crystal structure of apo human galactose mutarotase
Analyse Crystal structure of apo human galactose mutarotase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SNZ
- Type
- protein
- Length
- 686 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
- Q96C23
- Pockets
- 4 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aldose 1-epimerase (EC 5.1.3.3) | protein | 344 | 8% helix, 47% strand | Q96C23 |
| B | Aldose 1-epimerase (EC 5.1.3.3) | protein | 342 | 8% helix, 47% strand | Q96C23 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 199 | 0.56 | 0.79 | 32 | empty |
| 2 | 215 | 0.54 | 0.78 | 33 | empty |
| 3 | 97 | 0.37 | 0.75 | 22 | empty |
| 4 | 75 | 0.33 | 0.75 | 18 | empty |
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 Q96C23
- Elsewhere: RCSB PDB 1SNZ · PDBe 1SNZ · UniProt Q96C23
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