Research workbench
Human transforming growth factor beta 3, crystallized from peg 4000
Analyse Human transforming growth factor beta 3, crystallized from peg 4000 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TGK
- Type
- protein
- Length
- 112 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transforming growth factor beta 3
- UniProt
- P10600
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transforming growth factor beta 3 | protein | 112 | 18% helix, 38% strand | P10600 |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1TGK · Human transforming growth factor beta 3, crystallized from peg 4000 · the same entry in another collection · chain A against A, TM-score 1.00
- P10600 · AlphaFold monomer V2.0 prediction for transforming growth factor beta-3 proprotein… · a predicted model of the same protein · chain A against A, TM-score 0.82
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 P10600
- Elsewhere: RCSB PDB 1TGK · PDBe 1TGK · UniProt P10600
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