MolNFT v1 · #75076 · protein

Phosphofructokinase. structure and control

3PFK: “Phosphofructokinase. structure and control”. X-ray diffraction, 1 ligand (PO4), 2 pockets (best druggability 0.46). MolNFT v1 #75076 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3PFK
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: PO4
Pockets: 2 · best druggability 0.46

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphofructokinase (EC 2.7.1.11)	protein	319	46% helix, 19% strand	P00512

Ligands and binding sites

PO4 · Phosphate ion · ion · 2 copies · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	184	0.46	0.75	33	empty
2	83	0.35	0.76	18	empty

Compared structures

3PFK · 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 0.99

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 3PFK · PDBe 3PFK · UniProt P00512

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