Research workbench
Crystal structure of the E. coli type 1 pilus subunit FimG (engineered variant with substitution Q134E; N-terminal FimG residues 1-12 truncated) in complex with the donor strand peptide DsF_SRIRIRGYVR
Analyse Crystal structure of the E. coli type 1 pilus subunit FimG (engineered variant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5IQN
- Type
- protein
- Length
- 284 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1
- Source
- Escherichia coli K-12; SYNTHETIC CONSTRUCT
- Molecule
- Protein FimG; Protein FimF
- UniProt
- P08190, P08189
- Ligands
- CO
- Pockets
- 3 · best druggability 0.47
Structure
x-ray diffraction · resolution 1 · 2 distinct chains · 2% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, G | Protein FimG | protein | 132 | 2% helix, 50% strand | P08190 |
| B, F | Protein FimF | protein | 10 | 0% helix, 80% strand | P08189 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 153 | 0.47 | 0.77 | 28 | empty |
| 2 | 92 | 0.37 | 0.76 | 22 | CO |
| 3 | 54 | 0.30 | 0.76 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1046 Ų buried · 37 hydrogen bonds · protein-protein
- F–G · 1031 Ų buried · 35 hydrogen bonds · protein-protein
- A–G · 444 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5IQN · Crystal structure of the E. COLI type 1 pilus subunit fimg (engineered variant with… · the same entry in another collection · chain G against G, TM-score 1.00
- P08190 · AlphaFold monomer V2.0 prediction for protein fimg (P08190) · a predicted model of the same protein · chain A against A, TM-score 0.99
- P08189 · AlphaFold monomer V2.0 prediction for protein fimf (P08189) · a predicted model of the same protein · chain B against A, TM-score 0.71
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 P08190
- Every structure of UniProt P08189
- Elsewhere: RCSB PDB 5IQN · PDBe 5IQN · UniProt P08190 · UniProt P08189
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