Research workbench
A comparison of NMR solution structures of the receptor binding domains of pseudomonas aeruginosa pili strains pao, KB7, and pak: implications for receptor binding and synthetic vaccine design
Analyse A comparison of NMR solution structures of the receptor binding domains of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KB7
- Type
- protein
- Length
- 17 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- KB7 pilin, trans
- UniProt
- Q53391
- Ligands
- ACE
Structure
solution nmr · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | KB7 pilin, trans | protein | 17 | 0% helix, 0% strand | Q53391 |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent, 1 disulfide (covalent ligand, disulfide).
Compared structures
- 1KB7 · A comparison of NMR solution structures of the receptor binding domains of pseudomonas… · the same entry in another collection · chain A against A, TM-score 1.00
- Q53391 · AlphaFold monomer V2.0 prediction for fimbrial protein (Q53391) · a predicted model of the same protein · chain A against A, TM-score 0.22
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 Q53391
- Elsewhere: RCSB PDB 1KB7 · PDBe 1KB7 · UniProt Q53391
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