MolNFT v1 · #34842 · protein
Structural basis for the inhibition of insulin-like growth factors by igf binding proteins
2DSP · Insulin-like growth factor-binding protein 4: “Structural basis for the inhibition of insulin-like growth factors by igf binding proteins”. X-ray diffraction, 2 pockets (best druggability 0.53). MolNFT v1 #34842 on GenesisL1: 3D…
- PDB
- 2DSP
- Type
- protein
- Length
- 148 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin-like growth factor-binding protein 4; Insulin-like growth factor ib
- UniProt
- P22692, P05019
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Insulin-like growth factor-binding protein 4 | protein | 91 | 22% helix, 20% strand | P22692 |
| I | Insulin-like growth factor ib | protein | 57 | 51% helix, 11% strand | P05019 |
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 | 215 | 0.53 | 0.78 | 37 | empty |
| 2 | 80 | 0.37 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- B–I · 1077 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 disulfide (disulfide).
Compared structures
- 2DSP · Structural Basis for the Inhibition of Insulin-like Growth Factors by IGF Binding Proteins · the same entry in another collection · chain B against B, TM-score 1.00
- P22692 · AlphaFold monomer V2.0 prediction for insulin-like growth factor- binding protein 4… · a predicted model of the same protein · chain B against A, TM-score 0.97
- P05019 · AlphaFold monomer V2.0 prediction for insulin-like growth factor I (P05019) · a predicted model of the same protein · chain I against A, TM-score 0.80
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 P22692
- Every structure of UniProt P05019
- Elsewhere: RCSB PDB 2DSP · PDBe 2DSP · UniProt P22692 · UniProt P05019
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