Research workbench
Pseudomonas aeruginosa hdah bound to acetate.
Analyse Pseudomonas aeruginosa hdah bound to acetate. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5G0X
- Type
- protein
- Length
- 746 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9HXM1
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 370 | — | Q9HXM1 |
| C | — | protein | 376 | — | Q9HXM1 |
Compared structures
- Q9HXM1 · AlphaFold monomer V2.0 prediction for histone deacetylase-like amidohydrolase (Q9HXM1) · 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 Q9HXM1
- Elsewhere: RCSB PDB 5G0X · PDBe 5G0X · UniProt Q9HXM1
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