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Crystal structure of fimh lectin domain with the TYR48ALA mutation, in complex with heptyl alpha-D-mannopyrannoside

Analyse Crystal structure of fimh lectin domain with the TYR48ALA mutation, in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4CA4
Type: protein
Length: 316 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fimh
UniProt: A2IC68
Ligands: KGM
Pockets: 2 · best druggability 0.58

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

KGM · heptyl alpha-D-mannopyranoside · ligand · 2 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	147	0.58	0.83	27	empty
2	172	0.43	0.74	27	empty

Interfaces

1 interface between chains.

A–B · 545 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

4CA4 · Crystal structure of FimH lectin domain with the Tyr48Ala mutation, in complex with… · the same entry in another collection · chain A against A, TM-score 1.00

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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 4CA4 · PDBe 4CA4 · UniProt A2IC68

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