Research workbench

L-Fuculose-1-Phosphate Aldolase from Escherichia coli Mutant F131A

Analyse L-Fuculose-1-Phosphate Aldolase from Escherichia coli Mutant F131A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1DZW
Type: protein
Length: 206 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.17
Source: Escherichia coli
Molecule: L-fuculose phosphate aldolase
EC: 4.1.2.17
UniProt: A0A037YR34
Ligands: ZN, SO4
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · resolution 2.17 · 1 distinct chain · 44% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
P	L-fuculose phosphate aldolase (EC 4.1.2.17)	protein	206	44% helix, 17% strand	A0A037YR34

Ligands and binding sites

ZN · Zinc ion · metal · chains P
SO4 · Sulfate ion · ion · 2 copies · chains P
BME · Beta-mercaptoethanol · additive · chains P

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	76	0.43	0.80	17	SO4, BME

Modifications

Observed in the structure: 1 covalent (additive adduct).

Compared structures

1DZW · L-fuculose-1-phosphate aldolase from escherichia COLI mutant F131A · the same entry in another collection · chain P against P, 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 A0A037YR34
Elsewhere: RCSB PDB 1DZW · PDBe 1DZW · UniProt A0A037YR34

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.