Research workbench
Crystal structure analysis of yeast trapp associate protein TCA17
Analyse Crystal structure analysis of yeast trapp associate protein TCA17 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PR6
- Type
- protein
- Length
- 145 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trapp-associated protein TCA17
- UniProt
- P32613
- Ligands
- CL
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trapp-associated protein TCA17 | protein | 145 | 45% helix, 21% strand | P32613 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 modified (engineered, oxidation).
Compared structures
- 3PR6 · Crystal structure analysis of yeast TRAPP associate protein Tca17 · the same entry in another collection · chain A against A, TM-score 1.00
- P32613 · AlphaFold monomer V2.0 prediction for trapp-associated protein TCA17 (P32613) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 P32613
- Elsewhere: RCSB PDB 3PR6 · PDBe 3PR6 · UniProt P32613
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