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Crystal structure of the ECH2 decarboxylase domain of curf from lyngbya majuscula
Analyse Crystal structure of the ECH2 decarboxylase domain of curf from lyngbya… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q2X
- Type
- protein
- Length
- 242 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Curf
- UniProt
- Q6DNE7
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Curf | protein | 242 | 50% helix, 18% strand | Q6DNE7 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · 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 | 133 | 0.76 | 0.94 | 29 | GOL |
| 2 | 140 | 0.46 | 0.77 | 19 | empty |
| 3 | 90 | 0.40 | 0.78 | 21 | empty |
| 4 | 76 | 0.31 | 0.74 | 13 | empty |
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 2Q2X · Crystal Structure of the ECH2 decarboxylase domain of CurF from Lyngbya majuscula · the same entry in another collection · chain A against A, TM-score 1.00
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 Q6DNE7
- Elsewhere: RCSB PDB 2Q2X · PDBe 2Q2X · UniProt Q6DNE7
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