MolNFT v1 · #4979 · protein

L-fuculose 1-phosphate aldolase from escherichia COLI mutant DEL(27)

1E4A: “L-fuculose 1-phosphate aldolase from escherichia COLI mutant DEL(27)”. X-ray diffraction, 2 ligands (ZN, SO4), 1 pocket (best druggability 0.42). MolNFT v1 #4979 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1E4A
Type: protein
Length: 205 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L-fuculose 1-phosphate aldolase
EC: 4.1.2.17
UniProt: P11550
Ligands: ZN, SO4
Pockets: 1 · best druggability 0.42

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
P	L-fuculose 1-phosphate aldolase (EC 4.1.2.17)	protein	205	44% helix, 17% strand	P11550

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	72	0.42	0.80	18	SO4, BME

Modifications

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

Compared structures

1E4A · L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant Del(27) · 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 P11550
Elsewhere: RCSB PDB 1E4A · PDBe 1E4A · UniProt P11550

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