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Crystal structure of lectin domain of F9 pilus adhesin fmlh from E. COLI UTI89

Analyse Crystal structure of lectin domain of F9 pilus adhesin fmlh from E. COLI UTI89 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6AOW
Type: protein
Length: 302 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: F9 pilus adhesin fmlh
UniProt: Q1RBS0
Ligands: SO4
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	F9 pilus adhesin fmlh	protein	152	5% helix, 49% strand	Q1RBS0
B	F9 pilus adhesin fmlh	protein	150	4% helix, 49% strand	Q1RBS0

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A, 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	390	0.59	0.76	55	empty

Interfaces

1 interface between chains.

A–B · 547 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

6AOW · Crystal structure of lectin domain of F9 pilus adhesin FmlH from E. coli UTI89 · 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 Q1RBS0
Elsewhere: RCSB PDB 6AOW · PDBe 6AOW · UniProt Q1RBS0

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