Research workbench
Anti from P. luminescens catalyses terminal polyketide shortening in the biosynthesis of anthraquinones
Analyse Anti from P. luminescens catalyses terminal polyketide shortening in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HXA
- Type
- protein
- Length
- 375 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti
- UniProt
- Q7MZT8
- Pockets
- 1 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Anti | protein | 375 | 51% helix, 16% strand | Q7MZT8 |
Ligands and binding sites
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 | 137 | 0.69 | 0.89 | 32 | empty |
Compared structures
- 6HXA · AntI from P. luminescens catalyses terminal polyketide shortening in the biosynthesis of… · 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 Q7MZT8
- Elsewhere: RCSB PDB 6HXA · PDBe 6HXA · UniProt Q7MZT8
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