Research workbench
Crystal structure of alpk
Analyse Crystal structure of alpk in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6J0Z
- Type
- protein
- Length
- 488 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative angucycline-like polyketide oxygenase
- UniProt
- Q6VMI4
- Ligands
- FAD
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Putative angucycline-like polyketide oxygenase | protein | 488 | 29% helix, 23% strand | Q6VMI4 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1034 | 0.80 | 0.81 | 90 | FAD |
| 2 | 103 | 0.65 | 0.89 | 21 | empty |
| 3 | 54 | 0.51 | 0.87 | 19 | empty |
| 4 | 106 | 0.50 | 0.81 | 22 | empty |
| 5 | 118 | 0.47 | 0.79 | 23 | empty |
Compared structures
- 6J0Z · Crystal structure of AlpK · the same entry in another collection · chain C against C, 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 Q6VMI4
- Elsewhere: RCSB PDB 6J0Z · PDBe 6J0Z · UniProt Q6VMI4
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