MolNFT v1 · #86049 · protein

Crystal structure of apo fimh lectin domain at 1.5 a resolution

4AUU: “Crystal structure of apo fimh lectin domain at 1.5 a resolution”. X-ray diffraction, 2 ligands (NI, SO4), 1 pocket (best druggability 0.56). MolNFT v1 #86049 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4AUU
Type: protein
Length: 316 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fimh
UniProt: A2IC68
Ligands: NI, SO4
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Fimh	protein	158	6% helix, 53% strand	A2IC68

Ligands and binding sites

NI · Nickel (II) ion · metal · 2 copies · chains A, B
SO4 · Sulfate ion · ion · chains A
EDO · 1,2-ethanediol · 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	189	0.56	0.80	43	empty

Interfaces

1 interface between chains.

A–B · 543 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

4AUU · Crystal structure of apo FimH lectin domain at 1.5 A resolution · 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 A2IC68
Elsewhere: RCSB PDB 4AUU · PDBe 4AUU · UniProt A2IC68

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