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Crystal structure of acinetobacter baumannii CARO2
Analyse Crystal structure of acinetobacter baumannii CARO2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RLB
- Type
- protein
- Length
- 426 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbapenem-associated resistance protein
- UniProt
- Q5DL42
- Pockets
- 5 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 65% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Carbapenem-associated resistance protein | protein | 213 | 10% helix, 65% strand | Q5DL42 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 236 | 0.57 | 0.78 | 33 | empty |
| 2 | 114 | 0.57 | 0.84 | 25 | empty |
| 3 | 252 | 0.55 | 0.76 | 29 | empty |
| 4 | 92 | 0.46 | 0.80 | 21 | empty |
| 5 | 57 | 0.31 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 476 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 4RLB · Crystal structure of Acinetobacter baumannii CarO2 · 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 Q5DL42
- Elsewhere: RCSB PDB 4RLB · PDBe 4RLB · UniProt Q5DL42
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