Research workbench
Citrobacter freundii F448A mutant tyrosine phenol-lyase complexed with 4-hydroxypyridine and aminoacrylate from S-ethyl-L-cysteine
Analyse Citrobacter freundii F448A mutant tyrosine phenol-lyase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MQQ
- Type
- protein
- Length
- 912 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P31013
- Ligands
- CQG, K
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 456 | — | P31013 |
Ligands and binding sites
- CQG · pyridin-4-ol · ligand · 3 copies · chains A, B
- K · Potassium ion · metal · 2 copies · chains A, B
- P33 · 3,6,9,12,15,18-hexaoxaicosane-1,20-diol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6MQQ · Citrobacter freundii F448A mutant tyrosine phenol-lyase complexed with 4-hydroxypyridine… · the same entry in another collection · chain A against A, TM-score 1.00
- P31013 · AlphaFold monomer V2.0 prediction for tyrosine phenol-lyase (P31013) · a predicted model of the same protein · chain A 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 P31013
- Elsewhere: RCSB PDB 6MQQ · PDBe 6MQQ · UniProt P31013
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