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Crystal Structure of the O-Methyltransferase from the trans-AT PKS multienzyme C0ZGQ3 of Brevibacillus brevis
Analyse Crystal Structure of the O-Methyltransferase from the trans-AT PKS multienzyme… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HP1
- Type
- protein
- Length
- 297 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.9
- Source
- Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599)
- Molecule
- Putative polyketide synthase
- UniProt
- C0ZGQ3
- Ligands
- EMC
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · resolution 1.9 · 1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative polyketide synthase | protein | 297 | 42% helix, 21% strand | C0ZGQ3 |
Ligands and binding sites
- EMC · Ethyl mercury ion · ligand · 4 copies · 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 | 499 | 0.68 | 0.78 | 51 | EMC |
| 2 | 68 | 0.39 | 0.79 | 11 | empty |
| 3 | 102 | 0.36 | 0.74 | 20 | empty |
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 6HP1 · Crystal structure of the O-methyltransferase from the trans-at pks multienzyme C0ZGQ3 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 C0ZGQ3
- Elsewhere: RCSB PDB 6HP1 · PDBe 6HP1 · UniProt C0ZGQ3
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