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An unusual feature revealed by the crystal structure at 2.2 ångströms resolution of human transforming growth factor-BETA2
Analyse An unusual feature revealed by the crystal structure at 2.2 ångströms… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TFG
- Type
- protein
- Length
- 112 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transforming growth factor, beta 2
- UniProt
- P61812
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transforming growth factor, beta 2 | protein | 112 | 21% helix, 41% strand | P61812 |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1TFG · An unusual feature revealed by the crystal structure at 2.2 ångströms resolution of human… · the same entry in another collection · chain A against A, TM-score 1.00
- P61812 · AlphaFold monomer V2.0 prediction for transforming growth factor beta-2 proprotein… · a predicted model of the same protein · chain A against A, TM-score 0.92
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 P61812
- Elsewhere: RCSB PDB 1TFG · PDBe 1TFG · UniProt P61812
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