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Crystal structure of the beta subunit of the benzoate 1,2-dioxygenase (benb, BMAA0186) from burkholderia mallei atcc 23344 at 1.90 a resolution
Analyse Crystal structure of the beta subunit of the benzoate 1,2-dioxygenase (benb… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3E99
- Type
- protein
- Length
- 149 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Benzoate 1,2-dioxygenase beta subunit
- EC
- 1.14.12.10
- UniProt
- Q62E64
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Benzoate 1,2-dioxygenase beta subunit (EC 1.14.12.10) | protein | 149 | 28% helix, 45% strand | Q62E64 |
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: 3 modified (engineered).
Compared structures
- 3E99 · Crystal structure of the beta subunit of the benzoate 1,2-dioxygenase (benb, bmaa0186)… · 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 Q62E64
- Elsewhere: RCSB PDB 3E99 · PDBe 3E99 · UniProt Q62E64
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