Research workbench
Crystal structure of flu-tpr in complex with the C-terminal region of glutr
Analyse Crystal structure of flu-tpr in complex with the C-terminal region of glutr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4YVQ
- Type
- protein
- Length
- 203 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamyl-tRNA reductase 1, chloroplastic; Protein fluorescent in blue light, chloroplastic
- EC
- 1.2.1.70
- UniProt
- P42804, Q940U6
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamyl-tRNA reductase 1, chloroplastic (EC 1.2.1.70) | protein | 84 | 79% helix, 0% strand | P42804 |
| C | Protein fluorescent in blue light, chloroplastic | protein | 119 | 81% helix, 0% strand | Q940U6 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1055 | 0.76 | 0.78 | 65 | empty |
| 2 | 97 | 0.38 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–C · 889 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 4YVQ · Crystal Structure of FLU-TPR in Complex with the C-terminal Region of GluTR · the same entry in another collection · chain A against A, TM-score 1.00
- Q940U6 · AlphaFold monomer V2.0 prediction for protein fluorescent in blue light, chloroplastic… · a predicted model of the same protein · chain C against A, TM-score 0.98
- P42804 · AlphaFold monomer V2.0 prediction for glutamyl-tRNA reductase 1, chloroplastic (P42804) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P42804
- Every structure of UniProt Q940U6
- Elsewhere: RCSB PDB 4YVQ · PDBe 4YVQ · UniProt P42804 · UniProt Q940U6
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