Research workbench
Crystal structure of acinetobacter baumannii caro
Analyse Crystal structure of acinetobacter baumannii caro in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FUV
- Type
- protein
- Length
- 213 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Porin protein associated with imipenem resistance
- UniProt
- F0QP73
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 63% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Porin protein associated with imipenem resistance | protein | 213 | 11% helix, 63% strand | F0QP73 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
- C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 9 copies · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 192 | 0.49 | 0.76 | 24 | C8E |
| 2 | 64 | 0.44 | 0.82 | 21 | empty |
Compared structures
- 4FUV · Crystal Structure of Acinetobacter baumannii CarO · 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 F0QP73
- Elsewhere: RCSB PDB 4FUV · PDBe 4FUV · UniProt F0QP73
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.