Research workbench
Crystal structure of csuc-CSUA/B chaperone-major subunit pre-assembly complex from csu biofilm-mediating pili of acinetobacter baumannii
Analyse Crystal structure of csuc-CSUA/B chaperone-major subunit pre-assembly complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5D6H
- Type
- protein
- Length
- 321 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Csuc; CSUA/B
- UniProt
- Q6XBY4, Q6XBY7
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Csuc | protein | 223 | 9% helix, 50% strand | Q6XBY4 |
| B | CSUA/B | protein | 98 | 0% helix, 39% strand | Q6XBY7 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 567 | 0.74 | 0.81 | 72 | empty |
| 2 | 138 | 0.51 | 0.80 | 27 | empty |
| 3 | 85 | 0.34 | 0.75 | 16 | empty |
| 4 | 55 | 0.31 | 0.77 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1484 Ų buried · 25 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified, 1 disulfide (engineered, disulfide).
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 Q6XBY4
- Every structure of UniProt Q6XBY7
- Elsewhere: RCSB PDB 5D6H · PDBe 5D6H · UniProt Q6XBY4 · UniProt Q6XBY7
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