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Crystal structure of cyclohexadienyl dehydratase from pseudomonas aeruginosa bound to acetate
Analyse Crystal structure of cyclohexadienyl dehydratase from pseudomonas aeruginosa… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HPQ
- Type
- protein
- Length
- 238 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclohexadienyl dehydratase
- EC
- 4.2.1.51, 4.2.1.91
- UniProt
- Q01269
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclohexadienyl dehydratase (EC 4.2.1.51, 4.2.1.91) | protein | 238 | 38% helix, 23% strand | Q01269 |
Ligands and binding sites
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5HPQ · Crystal structure of cyclohexadienyl dehydratase from Pseudomonas aeruginosa bound to… · the same entry in another collection · chain A against A, TM-score 1.00
- Q01269 · AlphaFold monomer V2.0 prediction for cyclohexadienyl dehydratase (Q01269) · 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 Q01269
- Elsewhere: RCSB PDB 5HPQ · PDBe 5HPQ · UniProt Q01269
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