Research workbench
A de novo enzyme for the morita-baylis-hillman reaction BH32.6
Analyse A de novo enzyme for the morita-baylis-hillman reaction BH32.6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Z1K
- Type
- protein
- Length
- 231 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BH32.6 protein
- Ligands
- CA
- Pockets
- 1 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BH32.6 protein | protein | 231 | 54% helix, 14% strand | — |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
- FMT · Formic acid · additive · 2 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 705 | 0.81 | 0.85 | 59 | FMT |
Compared structures
- 6Z1K · A de novo Enzyme for the Morita-Baylis-Hillman Reaction BH32.6 · 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
- Elsewhere: RCSB PDB 6Z1K · PDBe 6Z1K
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