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The crystal structure of phosphofructokinase (LIN2199) from listeria innocua in complex with ATP at 1.6A

Analyse The crystal structure of phosphofructokinase (LIN2199) from listeria innocua in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3IE7
Type: protein
Length: 309 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: LIN2199 protein
EC: 2.7.1.-
UniProt: Q929S5
Ligands: ATP, MG
Pockets: 2 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	LIN2199 protein (EC 2.7.1.-)	protein	309	38% helix, 25% strand	Q929S5

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
MG · Magnesium ion · metal · 3 copies · chains A
GOL · Glycerol · additive · chains A

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	383	0.61	0.77	50	ATP, MG, GOL
2	62	0.46	0.83	12	empty

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

3IE7 · The crystal structure of phosphofructokinase (lin2199) from Listeria innocua in complex… · 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 Q929S5
Elsewhere: RCSB PDB 3IE7 · PDBe 3IE7 · UniProt Q929S5

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