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Structural characterization of tetrameric mycobacterium tuberculosis fructose 1,6-bisphosphate aldolase - substrate binding and catalysis mechanism of a class iia bacterial aldolase

Analyse Structural characterization of tetrameric mycobacterium tuberculosis fructose… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ELF
Type: protein
Length: 332 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fructose-bisphosphate aldolase
EC: 4.1.2.13
UniProt: P67475
Ligands: 2FP, ZN, NA
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fructose-bisphosphate aldolase (EC 4.1.2.13)	protein	332	50% helix, 13% strand	P67475

Ligands and binding sites

2FP · 1,6-fructose diphosphate (linear form) · ligand · chains A
ZN · Zinc ion · metal · 2 copies · chains A
NA · Sodium ion · metal · chains A

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	62	0.34	0.77	17	2FP

Compared structures

3ELF · Structural Characterization of tetrameric Mycobacterium tuberculosis fructose… · 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 P67475
Elsewhere: RCSB PDB 3ELF · PDBe 3ELF · UniProt P67475

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