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Long polar fimbriae adhesin lpfd from the adherent invasive E. COLI strain LF82

Analyse Long polar fimbriae adhesin lpfd from the adherent invasive E. COLI strain LF82 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5AFO
Type: protein
Length: 686 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fimbriae
UniProt: E2QGQ5
Pockets: 4 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Fimbriae	protein	343	2% helix, 52% strand	E2QGQ5

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	111	0.34	0.73	24	empty
2	95	0.33	0.73	31	empty
3	59	0.33	0.77	17	GOL
4	63	0.30	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 740 Å² buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

5AFO · Long Polar Fimbriae adhesin LpfD from the adherent invasive E. coli strain LF82 · the same entry in another collection · chain A against A, TM-score 1.00

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 E2QGQ5
Elsewhere: RCSB PDB 5AFO · PDBe 5AFO · UniProt E2QGQ5

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