Research workbench
Crystal structure of the mutant E494Q of GH92 alpha-1,2-mannosidase from enterococcus faecalis atcc 10100 in complex with alpha-1,2- mannobiose
Analyse Crystal structure of the mutant E494Q of GH92 alpha-1,2-mannosidase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7FE2
- Type
- protein
- Length
- 2,848 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A6N0WQ22
- Ligands
- BMA, MAN, CA, NA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 712 | — | A0A6N0WQ22 |
Ligands and binding sites
- BMA · beta-D-mannopyranose · sugar · 4 copies · chains A, B, C, D
- MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A, B, C, D
- CA · Calcium ion · metal · 4 copies · chains A, B, C, D
- NA · Sodium ion · metal · 4 copies · chains A, B, C, D
- EDO · 1,2-ethanediol · additive · 26 copies · chains A, B, C, D
- ACT · Acetate ion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7FE2 · Crystal structure of the mutant E494Q of GH92 alpha-1,2-mannosidase from Enterococcus… · 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 A0A6N0WQ22
- Elsewhere: RCSB PDB 7FE2 · PDBe 7FE2 · UniProt A0A6N0WQ22
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