Research workbench
Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions
Analyse Three-dimensional nuclear magnetic resonance structures of mouse epidermal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EPH
- 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, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Epidermal growth factor | protein | 53 | 0% helix, 15% strand | P01132 |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1EPH · Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor… · 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 0.53
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 1EPH · PDBe 1EPH · UniProt P01132
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