Research workbench
Crystal structure of biphenyl synthase from malus domestic complexed with benzoyl-CoA
Analyse Crystal structure of biphenyl synthase from malus domestic complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WC4
- Type
- protein
- Length
- 757 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- K9MST3
- Ligands
- BU4, BYC
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 379 | — | K9MST3 |
| B | — | protein | 378 | — | K9MST3 |
Ligands and binding sites
- BU4 · (3R)-butane-1,3-diol · ligand · 2 copies · chains A, B
- BYC · benzoyl coenzyme A · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5WC4 · Crystal structure of biphenyl synthase from Malus domestic complexed with benzoyl-CoA · 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 K9MST3
- Elsewhere: RCSB PDB 5WC4 · PDBe 5WC4 · UniProt K9MST3
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