Research workbench
Analysis of the solution structure of human interleukin 4 determined by heteronuclear three-dimensional nuclear magnetic resonance techniques
Analyse Analysis of the solution structure of human interleukin 4 determined by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ITM
- Type
- protein
- Length
- 130 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Interleukin-4
- UniProt
- P05112
Structure
solution nmr · 1 distinct chain · 60% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Interleukin-4 | protein | 130 | 60% helix, 3% strand | P05112 |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1ITM · Analysis of the solution structure of human interleukin 4 determined by heteronuclear… · the same entry in another collection · chain A against A, TM-score 1.00
- P05112 · AlphaFold monomer V2.0 prediction for interleukin-4 (P05112) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P05112
- Elsewhere: RCSB PDB 1ITM · PDBe 1ITM · UniProt P05112
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