Research workbench
ENDO180 D1-4, monoclinic form
Analyse ENDO180 D1-4, monoclinic form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AO5
- Type
- protein
- Length
- 869 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C-type mannose receptor 2
- UniProt
- Q9UBG0
- Ligands
- NA, SO4
- Pockets
- 8 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C-type mannose receptor 2 | protein | 435 | 14% helix, 33% strand | Q9UBG0 |
| B | C-type mannose receptor 2 | protein | 434 | 13% helix, 32% strand | Q9UBG0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 253 | 0.51 | 0.75 | 45 | empty |
| 2 | 158 | 0.47 | 0.76 | 21 | empty |
| 3 | 152 | 0.45 | 0.76 | 22 | empty |
| 4 | 97 | 0.44 | 0.79 | 20 | empty |
| 5 | 115 | 0.37 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 294 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 22 disulfide (disulfide).
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 Q9UBG0
- Elsewhere: RCSB PDB 5AO5 · PDBe 5AO5 · UniProt Q9UBG0
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