Research workbench
Crystal structure of amtb from E. COLI bound to topfluor cardiolipin
Analyse Crystal structure of amtb from E. COLI bound to topfluor cardiolipin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6B21
- Type
- protein
- Length
- 369 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ammonia channel
- UniProt
- P69681
- Ligands
- C9V
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 73% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ammonia channel | protein | 369 | 73% helix, 1% strand | P69681 |
Ligands and binding sites
- C9V · [(2R,5R,11R,14S,24E)-14-[(acetyloxy)methyl]-8-{[5-(3,5-dimethyl-1H-pyrrol-2-yl-kappan)-5-(3,5-dimethyl-2H-pyrrol-2-ylidene-kappan)pentanoyl]oxy}-5,11-dihydroxy-2-{[(9E)-octadec-9-enoyl]oxy}-5,11,16-trioxo-4,6,10, 12,15-pentaoxa-5lambda~5~,11lambda~5~-diphosphatritriacont-24-en-1-yl (9E)-octadec-9-enoatato](difluoro)boron · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 152 | 0.51 | 0.78 | 23 | empty |
| 2 | 154 | 0.47 | 0.77 | 22 | empty |
Compared structures
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 P69681
- Elsewhere: RCSB PDB 6B21 · PDBe 6B21 · UniProt P69681
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