Research workbench
Crystal structure of the cca-adding enzyme of a psychrophilic organism
Analyse Crystal structure of the cca-adding enzyme of a psychrophilic organism in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6QY6
- Type
- protein
- Length
- 373 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cca-adding enzyme
- EC
- 2.7.7.72
- UniProt
- A0A1C7DQ98
- Ligands
- PO4
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cca-adding enzyme (EC 2.7.7.72) | protein | 373 | 56% helix, 10% strand | A0A1C7DQ98 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
- ACT · Acetate ion · additive · 3 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 408 | 0.62 | 0.78 | 36 | ACT |
| 2 | 50 | 0.30 | 0.76 | 15 | empty |
Compared structures
- 6QY6 · Crystal structure of the CCA-adding enzyme of a psychrophilic organism · 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 A0A1C7DQ98
- Elsewhere: RCSB PDB 6QY6 · PDBe 6QY6 · UniProt A0A1C7DQ98
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