Research workbench
Crystal structure of native caib in complex with coenzyme a
Analyse Crystal structure of native caib in complex with coenzyme a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XVT
- Type
- protein
- Length
- 402 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Crotonobetainyl-COA:CARNITINE CoA-transferase
- EC
- 2.8.3.-
- UniProt
- P31572
- Ligands
- COA
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Crotonobetainyl-COA:CARNITINE CoA-transferase (EC 2.8.3.-) | protein | 402 | 38% helix, 18% strand | P31572 |
Ligands and binding sites
- COA · Coenzyme A · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 322 | 0.63 | 0.79 | 37 | COA |
| 2 | 90 | 0.41 | 0.78 | 21 | empty |
| 3 | 125 | 0.41 | 0.75 | 21 | empty |
Modifications
Observed in the structure: 16 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 P31572
- Elsewhere: RCSB PDB 1XVT · PDBe 1XVT · UniProt P31572
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