Research workbench
Structure of four truncated and mutated forms of quenching protein
Analyse Structure of four truncated and mutated forms of quenching protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DJM
- Type
- protein
- Length
- 457 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein suppressor of quenching 1, chloroplastic
- EC
- 3.1.3.-
- UniProt
- Q8VZ10
- Ligands
- NA
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein suppressor of quenching 1, chloroplastic (EC 3.1.3.-) | protein | 457 | 8% helix, 49% strand | Q8VZ10 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 428 | 0.72 | 0.82 | 37 | DTT, NA |
| 2 | 137 | 0.44 | 0.76 | 27 | empty |
| 3 | 97 | 0.33 | 0.73 | 19 | empty |
| 4 | 64 | 0.33 | 0.76 | 17 | empty |
Compared structures
- 7DJM · Structure of four truncated and mutated forms of quenching protein · the same entry in another collection · chain A against A, TM-score 1.00
- Q8VZ10 · AlphaFold monomer V2.0 prediction for protein suppressor of quenching 1, chloroplastic… · a predicted model of the same protein · chain A against A, TM-score 0.75
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 Q8VZ10
- Elsewhere: RCSB PDB 7DJM · PDBe 7DJM · UniProt Q8VZ10
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