Research workbench
IMP1 KH34
Analyse IMP1 KH34 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KRM
- Type
- protein
- Length
- 471 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin-like growth factor 2 mRNA-binding protein 1
- UniProt
- Q9NZI8
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 46% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin-like growth factor 2 mRNA-binding protein 1 | protein | 158 | 47% helix, 25% strand | Q9NZI8 |
| B | Insulin-like growth factor 2 mRNA-binding protein 1 | protein | 156 | 45% helix, 25% strand | Q9NZI8 |
| C | Insulin-like growth factor 2 mRNA-binding protein 1 | protein | 157 | 45% helix, 25% strand | Q9NZI8 |
Ligands and binding sites
- GOL · Glycerol · additive · 4 copies · chains A, C, B
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 | 982 | 0.80 | 0.82 | 71 | GOL |
| 2 | 350 | 0.55 | 0.74 | 37 | empty |
| 3 | 123 | 0.44 | 0.77 | 25 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1063 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 854 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 32 Ų buried · 0 hydrogen bonds · protein-protein
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 Q9NZI8
- Elsewhere: RCSB PDB 3KRM · PDBe 3KRM · UniProt Q9NZI8
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