Research workbench
Structure of apo unactivated igf-1R kinase domain at 1.5A resolution.
Analyse Structure of apo unactivated igf-1R kinase domain at 1.5A resolution. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1P4O
- Type
- protein
- Length
- 622 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin-like growth factor I receptor protein
- EC
- 2.7.1.112
- UniProt
- P08069
- Pockets
- 10 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin-like growth factor I receptor protein (EC 2.7.1.112) | protein | 308 | 42% helix, 18% strand | P08069 |
| B | Insulin-like growth factor I receptor protein (EC 2.7.1.112) | protein | 314 | 42% helix, 18% strand | P08069 |
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 644 | 0.63 | 0.74 | 64 | empty |
| 2 | 157 | 0.55 | 0.80 | 28 | empty |
| 3 | 140 | 0.53 | 0.81 | 27 | empty |
| 4 | 290 | 0.53 | 0.75 | 34 | empty |
| 5 | 126 | 0.44 | 0.76 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 1501 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 1P4O · Structure of Apo unactivated IGF-1R KInase domain at 1.5A resolution. · the same entry in another collection · chain A against A, TM-score 1.00
- P08069 · AlphaFold monomer V2.0 prediction for insulin-like growth factor 1 receptor (P08069) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P08069
- Elsewhere: RCSB PDB 1P4O · PDBe 1P4O · UniProt P08069
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