MolNFT v1 · #24368 · protein

Drae adhesin from escherichia COLI

1UT1 · Dr hemagglutinin structural subunit: “Drae adhesin from escherichia COLI”. X-ray diffraction, 1 ligand (SO4), 7 pockets (best druggability 0.56). MolNFT v1 #24368 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1UT1
Type: protein
Length: 836 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dr hemagglutinin structural subunit
UniProt: P24093
Ligands: SO4
Pockets: 7 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 60% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, E	Dr hemagglutinin structural subunit	protein	140	4% helix, 60% strand	P24093
B, C, D, F	Dr hemagglutinin structural subunit	protein	139	4% helix, 60% strand	P24093

Ligands and binding sites

SO4 · Sulfate ion · ion · 12 copies · chains A, E, B, F, C, D
EDO · 1,2-ethanediol · additive · 30 copies · chains A, D, F, E, B, C

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

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	405	0.56	0.74	49	EDO
2	327	0.51	0.73	43	EDO
3	214	0.46	0.74	32	EDO
4	175	0.44	0.74	26	EDO
5	123	0.39	0.75	22	EDO

Interfaces

9 interfaces between chains.

B–F · 723 Å² buried · 15 hydrogen bonds · protein-protein
D–E · 715 Å² buried · 16 hydrogen bonds · protein-protein
A–E · 713 Å² buried · 18 hydrogen bonds · protein-protein
C–F · 698 Å² buried · 16 hydrogen bonds · protein-protein
B–C · 697 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

1UT1 · DraE adhesin from Escherichia Coli · the same entry in another collection · chain F against F, TM-score 1.00
P24093 · AlphaFold monomer V2.0 prediction for dr hemagglutinin structural subunit (P24093) · a predicted model of the same protein · chain E 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 P24093
Elsewhere: RCSB PDB 1UT1 · PDBe 1UT1 · UniProt P24093

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