Research workbench
Structure of CFA/I pili chaperone-major subunit complex (cfaa-cfab)
Analyse Structure of CFA/I pili chaperone-major subunit complex (cfaa-cfab) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Y2O
- Type
- protein
- Length
- 353 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CFA/I fimbrial subunit a (colonization factor antigen subunit a putative chaperone)…
- UniProt
- E3PPC3, E3PPC4
- Ligands
- NI
- Pockets
- 7 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CFA/I fimbrial subunit a (colonization factor antigen subunit a putative chaperone) | protein | 211 | 0% helix, 52% strand | E3PPC3 |
| B | CFA/I fimbrial subunit B | protein | 142 | 0% helix, 32% strand | E3PPC4 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · 2 copies · chains B
- PGE · Triethylene glycol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 611 | 0.70 | 0.79 | 45 | NI |
| 2 | 66 | 0.70 | 0.95 | 20 | empty |
| 3 | 195 | 0.65 | 0.84 | 34 | empty |
| 4 | 109 | 0.60 | 0.86 | 28 | empty |
| 5 | 177 | 0.55 | 0.80 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 1683 Ų buried · 25 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4Y2O · Structure of CFA/I pili chaperone-major subunit complex (CfaA-CfaB) · the same entry in another collection · chain A against A, TM-score 1.00
- E3PPC4 · AlphaFold monomer V2.0 prediction for CFA/I fimbrial subunit B (E3PPC4) · a predicted model of the same protein · chain B against A, TM-score 0.82
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 E3PPC3
- Every structure of UniProt E3PPC4
- Elsewhere: RCSB PDB 4Y2O · PDBe 4Y2O · UniProt E3PPC3 · UniProt E3PPC4
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