Research workbench
Structure of the quorum quenching lactonase from alicyclobacillus acidoterrestris bound to a phosphate anion
Analyse Structure of the quorum quenching lactonase from alicyclobacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CGY
- Type
- protein
- Length
- 827 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- T0BMH6
- Ligands
- CO, PO4
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, H | — | protein | 276 | — | T0BMH6 |
| L | — | protein | 275 | — | T0BMH6 |
Ligands and binding sites
- CO · Cobalt (II) ion · metal · 6 copies · chains A, H, L
- PO4 · Phosphate ion · ion · 3 copies · chains A, H, L
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, H, L
- GOL · Glycerol · additive · 2 copies · chains A, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6CGY · Structure of the Quorum Quenching lactonase from Alicyclobacillus acidoterrestris bound… · 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 T0BMH6
- Elsewhere: RCSB PDB 6CGY · PDBe 6CGY · UniProt T0BMH6
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