Research workbench
Cryo-EM structure of archaic chaperone-usher csu pilus of acinetobacter baumannii
Analyse Cryo-EM structure of archaic chaperone-usher csu pilus of acinetobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ZL4
- Type
- protein
- Length
- 465 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CSUA/B
- UniProt
- A0A6F8TDQ5
- Pockets
- 2 · best druggability 0.47
Structure
electron microscopy · 3 distinct chains · 0% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CSUA/B | protein | 141 | 0% helix, 51% strand | A0A6F8TDQ5 |
| B, C | CSUA/B | protein | 155 | 0% helix, 54% strand | A0A6F8TDQ5 |
| D | CSUA/B | protein | 14 | 0% helix, 79% strand | A0A6F8TDQ5 |
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 | 219 | 0.47 | 0.74 | 33 | empty |
| 2 | 215 | 0.46 | 0.74 | 31 | empty |
Interfaces
5 interfaces between chains.
- A–B · 1787 Ų buried · 52 hydrogen bonds · protein-protein
- B–C · 1783 Ų buried · 52 hydrogen bonds · protein-protein
- C–D · 1282 Ų buried · 40 hydrogen bonds · protein-protein
- A–C · 234 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 233 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 7ZL4 · Cryo-EM structure of archaic chaperone-usher Csu pilus of Acinetobacter baumannii · 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 A0A6F8TDQ5
- Elsewhere: RCSB PDB 7ZL4 · PDBe 7ZL4 · UniProt A0A6F8TDQ5
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