Research workbench
Human iduronidase apo structure P21 form
Analyse Human iduronidase apo structure P21 form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MJ4
- Type
- protein
- Length
- 603 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-L-iduronidase
- EC
- 3.2.1.76
- UniProt
- P35475
- Ligands
- NAG, MAN, BMA, CL
- Pockets
- 7 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-L-iduronidase (EC 3.2.1.76) | protein | 603 | 25% helix, 31% strand | P35475 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 2 copies
- BMA · beta-D-mannopyranose · sugar · chains A
- CL · Chloride ion · ion · chains A
- GOL · Glycerol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.70 | 0.95 | 27 | empty |
| 2 | 158 | 0.60 | 0.83 | 20 | empty |
| 3 | 169 | 0.52 | 0.80 | 37 | GOL |
| 4 | 127 | 0.47 | 0.78 | 20 | GOL |
| 5 | 117 | 0.40 | 0.75 | 18 | empty |
Modifications
Observed in the structure: 3 glycan (N-glycosylation).
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 P35475
- Elsewhere: RCSB PDB 4MJ4 · PDBe 4MJ4 · UniProt P35475
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