Research workbench
Co-crystal structure of ORF2 an aromatic prenyl transferase from streptomyces sp. strain CL190 complexed with gspp and 1,6-dihydroxynaphtalene
Analyse Co-crystal structure of ORF2 an aromatic prenyl transferase from streptomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZB6
- Type
- protein
- Length
- 301 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aromatic prenyltransferase
- Ligands
- GST, DIN, MG, NO3
- Pockets
- 1 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aromatic prenyltransferase | protein | 301 | 37% helix, 24% strand | — |
Ligands and binding sites
- GST · Geranyl S-thiolodiphosphate · ligand · chains A
- DIN · 1,6-dihydroxy naphthalene · ligand · chains A
- MG · Magnesium ion · metal · chains A
- NO3 · Nitrate ion · ion · 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 | 660 | 0.82 | 0.86 | 71 | MG, GST, DIN |
Compared structures
- 1ZB6 · Co-Crystal Structure of ORF2 an Aromatic Prenyl Transferase from Streptomyces sp. strain… · 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 1ZB6 · PDBe 1ZB6
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.