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A ternary complex of hydroxycinnamoyl-CoA hydratase-lyase (hchl) with acetyl-coenzyme a and vanillin gives insights into substrate specificity and mechanism.
Analyse A ternary complex of hydroxycinnamoyl-CoA hydratase-lyase (hchl) with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VSU
- Type
- protein
- Length
- 1,475 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O69762
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 240 | — | O69762 |
| B | — | protein | 247 | — | O69762 |
| C | — | protein | 251 | — | O69762 |
| D | — | protein | 247 | — | O69762 |
| E | — | protein | 245 | — | O69762 |
| F | — | protein | 245 | — | O69762 |
Compared structures
- 2VSU · A ternary complex of Hydroxycinnamoyl-CoA Hydratase-Lyase (HCHL) with acetyl-Coenzyme A… · the same entry in another collection · chain E against E, TM-score 1.00
- O69762 · AlphaFold monomer V2.0 prediction for hydroxycinnamoyl-CoA hydratase- lyase (O69762) · a predicted model of the same protein · chain D against A, TM-score 0.99
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 O69762
- Elsewhere: RCSB PDB 2VSU · PDBe 2VSU · UniProt O69762
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