Research workbench
Crystal structure of the mutant of hpab (T198I, A276G, and R466H) complexed with FAD
Analyse Crystal structure of the mutant of hpab (T198I, A276G, and R466H) complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YYL
- Type
- protein
- Length
- 476 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-hydroxyphenylacetate-3-hydroxylase
- EC
- 1.14.13.3
- UniProt
- Q5SJP8
- Ligands
- FAD, SO4
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-hydroxyphenylacetate-3-hydroxylase (EC 1.14.13.3) | protein | 476 | 54% helix, 15% strand | Q5SJP8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 713 | 0.75 | 0.81 | 58 | FAD |
Compared structures
- 2YYL · Crystal structure of the mutant of HpaB (T198I, A276G, and R466H) complexed with FAD · the same entry in another collection · chain A against A, TM-score 1.00
- Q5SJP8 · AlphaFold monomer V2.0 prediction for 4-hydroxyphenylacetate 3-monooxygenase oxygenase… · a predicted model of the same protein · 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 Q5SJP8
- Elsewhere: RCSB PDB 2YYL · PDBe 2YYL · UniProt Q5SJP8
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