Research workbench
Solution structure of murine epidermal growth factor determined by NMR spectroscopy and refined by energy minimization with restraints
Analyse Solution structure of murine epidermal growth factor determined by NMR… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EGF
- Type
- protein
- Length
- 53 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epidermal growth factor
- UniProt
- P01132
Structure
solution nmr · 1 distinct chain · 0% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Epidermal growth factor | protein | 53 | 0% helix, 21% strand | P01132 |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 3EGF · Solution structure of murine epidermal growth factor determined by NMR spectroscopy and… · the same entry in another collection · chain A against A, TM-score 1.00
- P01132 · AlphaFold monomer V2.0 prediction for pro-epidermal growth factor (P01132) · a predicted model of the same protein · chain A against A, TM-score 0.59
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 P01132
- Elsewhere: RCSB PDB 3EGF · PDBe 3EGF · UniProt P01132
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