Research workbench
Structure of fima type-1 (FIMA1) prepilin of the type V major fimbrium
Analyse Structure of fima type-1 (FIMA1) prepilin of the type V major fimbrium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JZK
- Type
- protein
- Length
- 690 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major fimbrium subunit fima type-1
- UniProt
- B2RH54
- Ligands
- SRT, SO4
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Major fimbrium subunit fima type-1 | protein | 350 | 8% helix, 44% strand | B2RH54 |
| B | Major fimbrium subunit fima type-1 | protein | 340 | 6% helix, 45% strand | B2RH54 |
Ligands and binding sites
- SRT · S,R meso-tartaric acid · ligand · chains B
- SO4 · Sulfate ion · ion · chains B
- GOL · Glycerol · additive
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.52 | 0.83 | 23 | empty |
| 2 | 171 | 0.46 | 0.76 | 38 | empty |
| 3 | 63 | 0.31 | 0.75 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 461 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 6JZK · Structure of FimA type-1 (FimA1) prepilin of the type V major fimbrium · the same entry in another collection · chain A against A, TM-score 1.00
- B2RH54 · AlphaFold monomer V2.0 prediction for major fimbrium subunit fima type-1 (B2RH54) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 B2RH54
- Elsewhere: RCSB PDB 6JZK · PDBe 6JZK · UniProt B2RH54
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