MolNFT v1 · #34844 · protein
Structural basis for the inhibition of insulin-like growth factors by igf binding proteins
2DSR: “Structural basis for the inhibition of insulin-like growth factors by igf binding proteins”. X-ray diffraction. MolNFT v1 #34844 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2DSR
- Type
- protein
- Length
- 219 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P22692, P05019
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| G | — | protein | 79 | — | P22692 |
| B | — | protein | 80 | — | P22692 |
| I | — | protein | 60 | — | P05019 |
Compared structures
- 2DSR · Structural Basis for the Inhibition of Insulin-like Growth Factors by IGF Binding Proteins · the same entry in another collection · chain G against G, 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 0.75
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 2DSR · PDBe 2DSR · UniProt P22692 · UniProt P05019
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