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Crystal structure of agga, the major subunit of aggregative adherence fimbriae type I (AAF/I) from the escherichia COLI O4H104

Analyse Crystal structure of agga, the major subunit of aggregative adherence fimbriae… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4PH8
Type: protein
Length: 300 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aggregative adherence fimbrial subunit agga
UniProt: G5TBZ9
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Aggregative adherence fimbrial subunit agga	protein	150	9% helix, 51% strand	G5TBZ9

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

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	249	0.50	0.75	36	empty

Interfaces

1 interface between chains.

A–B · 487 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

4PH8 · Crystal structure of AggA, the major subunit of aggregative adherence fimbriae type I… · 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 G5TBZ9
Elsewhere: RCSB PDB 4PH8 · PDBe 4PH8 · UniProt G5TBZ9

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