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Afae-3 adhesin from escherichia COLI

Analyse Afae-3 adhesin from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1UT2
Type: protein
Length: 1,251 residues
Chains: 9
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Afimbrial adhesin afa-III
UniProt: Q57254
Ligands: SO4
Pockets: 8 · best druggability 0.80

Structure

x-ray diffraction · 3 distinct chains · 4% helix, 59% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Afimbrial adhesin afa-III	protein	138	4% helix, 59% strand	Q57254
B, C, D, E, F, G, I	Afimbrial adhesin afa-III	protein	139	4% helix, 59% strand	Q57254
H	Afimbrial adhesin afa-III	protein	140	2% helix, 58% strand	Q57254

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains D, A, H, I

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	922	0.80	0.82	121	empty
2	709	0.71	0.78	62	empty
3	398	0.63	0.78	46	empty
4	323	0.62	0.79	41	empty
5	144	0.48	0.78	24	empty

Interfaces

16 interfaces between chains.

G–H · 706 Å² buried · 13 hydrogen bonds · protein-protein
B–C · 692 Å² buried · 14 hydrogen bonds · protein-protein
F–H · 688 Å² buried · 16 hydrogen bonds · protein-protein
A–B · 679 Å² buried · 17 hydrogen bonds · protein-protein
E–I · 674 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 disulfide (disulfide).

Compared structures

1UT2 · AfaE-3 adhesin from Escherichia Coli · the same entry in another collection · chain I against I, TM-score 1.00
Q57254 · AlphaFold monomer V2.0 prediction for afimbrial adhesin afa-III (Q57254) · a predicted model of the same protein · chain D against A, TM-score 0.99

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 Q57254
Elsewhere: RCSB PDB 1UT2 · PDBe 1UT2 · UniProt Q57254

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