Research workbench
Crystal structure of dienelactone hydrolase (YP_324580.1) from anabaena variabilis atcc 29413 at 1.92 a resolution
Analyse Crystal structure of dienelactone hydrolase (YP_324580.1) from anabaena… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O2G
- Type
- protein
- Length
- 216 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dienelactone hydrolase
- UniProt
- Q3M5Q1
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dienelactone hydrolase | protein | 216 | 40% helix, 25% strand | Q3M5Q1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 2O2G · Crystal structure of Dienelactone hydrolase (YP_324580.1) from Anabaena variabilis ATCC… · the same entry in another collection · 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 Q3M5Q1
- Elsewhere: RCSB PDB 2O2G · PDBe 2O2G · UniProt Q3M5Q1
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