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Structure and mechanism of fibronectin binding and biofilm formation of enteroaggregative escherischia COLI aaf fimbriae

Analyse Structure and mechanism of fibronectin binding and biofilm formation of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4OR1
Type: protein
Length: 263 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Invasin homolog aafb, major fimbrial subunit of aggregative adherence fimbria II aafa…
UniProt: Q9X4L4, O30595
Ligands: SO4
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 0% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Invasin homolog aafb, major fimbrial subunit of aggregative adherence fimbria II aafa chimeric construct	protein	129	0% helix, 57% strand	Q9X4L4, O30595
B	Invasin homolog aafb, major fimbrial subunit of aggregative adherence fimbria II aafa chimeric construct	protein	134	0% helix, 56% strand	Q9X4L4, O30595

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A, B
ACT · Acetate ion · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	951	0.74	0.77	81	SO4

Interfaces

1 interface between chains.

A–B · 243 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

4OR1 · Structure and mechanism of fibronectin binding and biofilm formation of enteroaggregative… · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt Q9X4L4
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Elsewhere: RCSB PDB 4OR1 · PDBe 4OR1 · UniProt Q9X4L4 · UniProt O30595

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