Research workbench
Crystal structure of bacillus stearothermophilus cca-adding enzyme
Analyse Crystal structure of bacillus stearothermophilus cca-adding enzyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MIV
- Type
- protein
- Length
- 790 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TRNA cca-adding enzyme
- UniProt
- Q7SIB1
- Ligands
- MG
- Pockets
- 6 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | TRNA cca-adding enzyme | protein | 395 | 55% helix, 11% strand | Q7SIB1 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 473 | 0.60 | 0.75 | 45 | empty |
| 2 | 465 | 0.59 | 0.75 | 36 | empty |
| 3 | 96 | 0.33 | 0.73 | 18 | empty |
| 4 | 82 | 0.30 | 0.73 | 13 | empty |
| 5 | 51 | 0.27 | 0.74 | 12 | MG |
Interfaces
1 interface between chains.
- A–B · 496 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 modified (engineered).
Compared structures
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 Q7SIB1
- Elsewhere: RCSB PDB 1MIV · PDBe 1MIV · UniProt Q7SIB1
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