Research workbench
Chimeric carminomycin-4-O-methyltransferase (dnrk) with a region from 10-hydroxylase calmb
Analyse Chimeric carminomycin-4-O-methyltransferase (dnrk) with a region from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OWB
- Type
- protein
- Length
- 333 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carminomycin 4-O-methyltransferase DNRK,METHYLTRANSFERASE domain-containing protein
- EC
- 2.1.1.292
- UniProt
- Q06528, A0A2V2Q0Q4
- Ligands
- 3VL, SAH
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carminomycin 4-O-methyltransferase DNRK,METHYLTRANSFERASE domain-containing protein (EC 2.1.1.292) | protein | 333 | 48% helix, 17% strand | Q06528, A0A2V2Q0Q4 |
Ligands and binding sites
- 3VL · methyl (1R,2R,4S)-2-ethyl-2,5,7-trihydroxy-6,11-dioxo-4-{[2,3,6-trideoxy-3-(dimethylamino)-alpha-L-lyxo-hexopyranosyl]oxy}-1,2,3,4,6,11-hexahydrotetracene-1-carboxylate · ligand · chains A
- SAH · S-adenosyl-L-homocysteine · ligand · 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 | 829 | 0.80 | 0.82 | 76 | 3VL, SAH |
| 2 | 65 | 0.29 | 0.73 | 12 | empty |
| 3 | 66 | 0.28 | 0.73 | 10 | empty |
Compared structures
- 7OWB · Chimeric carminomycin-4-O-methyltransferase (DnrK) with a region from 10-hydroxylase CalMB · the same entry in another collection · chain A against A, TM-score 1.00
- Q06528 · AlphaFold monomer V2.0 prediction for carminomycin 4-O-methyltransferase dnrk (Q06528) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q06528
- Every structure of UniProt A0A2V2Q0Q4
- Elsewhere: RCSB PDB 7OWB · PDBe 7OWB · UniProt Q06528 · UniProt A0A2V2Q0Q4
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