Research workbench
Structure of human IGF2R domains 11-12
Analyse Structure of human IGF2R domains 11-12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V5N
- Type
- protein
- Length
- 271 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cation-independent mannose-6-phosphate receptor
- UniProt
- P11717
- Ligands
- NAG
- Pockets
- 2 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cation-independent mannose-6-phosphate receptor | protein | 271 | 3% helix, 43% strand | P11717 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
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 | 161 | 0.61 | 0.84 | 28 | empty |
| 2 | 151 | 0.43 | 0.75 | 20 | empty |
Modifications
Observed in the structure: 8 disulfide, 4 modified, 2 glycan (disulfide, engineered, 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 P11717
- Elsewhere: RCSB PDB 2V5N · PDBe 2V5N · UniProt P11717
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