Research workbench
Insulin-like growth factor-I bound to a phage-derived peptide
Analyse Insulin-like growth factor-I bound to a phage-derived peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PMX
- Type
- protein
- Length
- 86 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin-like growth factor ib; Igf-1 antagonist F1-1
- UniProt
- P05019
Structure
solution nmr · 2 distinct chains · 36% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin-like growth factor ib | protein | 70 | 33% helix, 0% strand | P05019 |
| B | Igf-1 antagonist F1-1 | protein | 16 | 50% helix, 0% strand | — |
Interfaces
1 interface between chains.
- A–B · 499 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1PMX · Insulin-like growth factor-I bound to a phage-derived peptide · the same entry in another collection · chain A against A, TM-score 1.00
- P05019 · AlphaFold monomer V2.0 prediction for insulin-like growth factor I (P05019) · a predicted model of the same protein · chain A against A, TM-score 0.64
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 P05019
- Elsewhere: RCSB PDB 1PMX · PDBe 1PMX · UniProt P05019
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