Research workbench
Solution structure of the FAS1 domain of human transforming growth factor-beta induced protein ig-H3
Analyse Solution structure of the FAS1 domain of human transforming growth factor-beta… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1X3B
- Type
- protein
- Length
- 146 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transforming growth factor-beta induced protein ig-H3
- UniProt
- Q15582
Structure
solution nmr · 1 distinct chain · 30% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transforming growth factor-beta induced protein ig-H3 | protein | 146 | 30% helix, 21% strand | Q15582 |
Compared structures
- 1X3B · Solution structure of the FAS1 domain of human transforming growth factor-beta induced… · the same entry in another collection · chain A against A, TM-score 1.00
- Q15582 · AlphaFold monomer V2.0 prediction for transforming growth factor- beta-induced protein… · a predicted model of the same protein · chain A against A, TM-score 0.90
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 Q15582
- Elsewhere: RCSB PDB 1X3B · PDBe 1X3B · UniProt Q15582
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