MolNFT v1 · #103397 · protein

Phosphofructokinase. structure and control

4PFK: “Phosphofructokinase. structure and control”. X-ray diffraction, 3 ligands (ADP, F6P, MG), 3 pockets (best druggability 0.51). MolNFT v1 #103397 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4PFK
Type: protein
Length: 319 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphofructokinase
EC: 2.7.1.11
UniProt: P00512
Ligands: ADP, F6P, MG
Pockets: 3 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphofructokinase (EC 2.7.1.11)	protein	319	45% helix, 19% strand	P00512

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A
F6P · 6-O-phosphono-beta-D-fructofuranose · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A

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

Pockets

3 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	188	0.51	0.78	32	F6P, MG, ADP
2	82	0.42	0.78	14	empty
3	80	0.34	0.75	18	empty

Compared structures

4PFK · Phosphofructokinase. structure and control · the same entry in another collection · chain A against A, TM-score 1.00
P00512 · AlphaFold monomer V2.0 prediction for ATP-dependent 6-phosphofructokinase (P00512) · a predicted model of the same protein · 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 P00512
Elsewhere: RCSB PDB 4PFK · PDBe 4PFK · UniProt P00512

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