Research workbench
Human cation-independent mannose 6-phosphate/ IGF2 receptor domain 8
Analyse Human cation-independent mannose 6-phosphate/ IGF2 receptor domain 8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Z31
- Type
- protein
- Length
- 278 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cation-independent mannose-6-phosphate receptor
- UniProt
- P11717
- Ligands
- NA, CL
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cation-independent mannose-6-phosphate receptor | protein | 139 | 4% helix, 42% strand | P11717 |
| B | Cation-independent mannose-6-phosphate receptor | protein | 139 | 4% helix, 45% strand | P11717 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 241 | 0.56 | 0.78 | 38 | empty |
| 2 | 246 | 0.54 | 0.76 | 34 | empty |
| 3 | 53 | 0.34 | 0.78 | 14 | CL |
Interfaces
1 interface between chains.
- A–B · 780 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 6Z31 · Human cation-independent mannose 6-phosphate/ IGF2 receptor domain 8 · the same entry in another collection · chain A against A, TM-score 1.00
- P11717 · AlphaFold monomer V2.0 prediction for cation-independent mannose-6-phosphate receptor… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P11717
- Elsewhere: RCSB PDB 6Z31 · PDBe 6Z31 · UniProt P11717
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