Research workbench
Crystal structures and enzymatic mechanisms of a populus tomentosa 4- coumarate--CoA ligase
Analyse Crystal structures and enzymatic mechanisms of a populus tomentosa 4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3A9U
- Type
- protein
- Length
- 523 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-coumarate--CoA ligase
- EC
- 6.2.1.12
- UniProt
- Q941M3
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-coumarate--CoA ligase (EC 6.2.1.12) | protein | 523 | 30% helix, 24% strand | Q941M3 |
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 | 727 | 0.77 | 0.82 | 105 | empty |
| 2 | 55 | 0.30 | 0.76 | 17 | empty |
| 3 | 54 | 0.27 | 0.74 | 11 | empty |
Compared structures
- 3A9U · Crystal structures and enzymatic mechanisms of a Populus tomentosa 4-coumarate--CoA ligase · 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 Q941M3
- Elsewhere: RCSB PDB 3A9U · PDBe 3A9U · UniProt Q941M3
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