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Extracellular ALPHA/BETA-hydrolase from paenibacillus species shares structural and functional homology to tobacco salicylic acid binding protein 2
Analyse Extracellular ALPHA/BETA-hydrolase from paenibacillus species shares structural… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TJ2
- Type
- protein
- Length
- 728 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A264DUQ2
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 243 | — | A0A264DUQ2 |
| C | — | protein | 242 | — | A0A264DUQ2 |
Compared structures
- 6TJ2 · Extracellular alpha/beta-hydrolase from Paenibacillus species shares structural and… · the same entry in another collection · chain B against B, 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 A0A264DUQ2
- Elsewhere: RCSB PDB 6TJ2 · PDBe 6TJ2 · UniProt A0A264DUQ2
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