Research workbench
Crystal structure of human class I ALPHA1,2-mannosidase
Analyse Crystal structure of human class I ALPHA1,2-mannosidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FMI
- Type
- protein
- Length
- 456 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoplasmic reticulum alpha-mannosidase I
- EC
- 3.2.1.113
- UniProt
- Q9UKM7
- Ligands
- CA, SO4
- Pockets
- 2 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoplasmic reticulum alpha-mannosidase I (EC 3.2.1.113) | protein | 456 | 49% helix, 13% strand | Q9UKM7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 201 | 0.61 | 0.82 | 24 | CA |
| 2 | 53 | 0.43 | 0.83 | 17 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1FMI · Crystal structure of human class I ALPHA1,2-mannosidase · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UKM7 · AlphaFold monomer V2.0 prediction for endoplasmic reticulum mannosyl- oligosaccharide… · a predicted model of the same protein · chain A 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 Q9UKM7
- Elsewhere: RCSB PDB 1FMI · PDBe 1FMI · UniProt Q9UKM7
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