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Crystal structure of self-complemented CSUA/B major subunit from archaic chaperone-usher csu pili of acinetobacter baumannii
Analyse Crystal structure of self-complemented CSUA/B major subunit from archaic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FM5
- Type
- protein
- Length
- 157 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CSUA/B,CSUA/B,CSUA/B,CSUA/B
- UniProt
- Q6XBY7
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CSUA/B,CSUA/B,CSUA/B,CSUA/B | protein | 157 | 0% helix, 54% strand | Q6XBY7 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6FM5 · Crystal structure of self-complemented CsuA/B major subunit from archaic chaperone-usher… · 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 Q6XBY7
- Elsewhere: RCSB PDB 6FM5 · PDBe 6FM5 · UniProt Q6XBY7
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