Research workbench
Crystal structure of gcoa F169A bound to syringol
Analyse Crystal structure of gcoa F169A bound to syringol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HQQ
- Type
- protein
- Length
- 402 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450
- UniProt
- A0A076MY51
- Ligands
- HEM, 3DM
- Pockets
- 3 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 | protein | 402 | 57% helix, 11% strand | A0A076MY51 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- 3DM · 2,6-dimethoxyphenol · 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 | 391 | 0.87 | 0.95 | 56 | HEM, 3DM |
| 2 | 82 | 0.38 | 0.78 | 15 | empty |
| 3 | 76 | 0.33 | 0.75 | 13 | empty |
Compared structures
- 6HQQ · Crystal structure of GcoA F169A bound to syringol · 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 A0A076MY51
- Elsewhere: RCSB PDB 6HQQ · PDBe 6HQQ · UniProt A0A076MY51
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