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MolNFT v1 · #12102 · protein

Crystal structure of human liver 6-phosphofructo-2-KINASE/FRUCTOSE-2, 6-bisphosphatase

1K6M · 6-phosphofructo-2-KINASE/FRUCTOSE-2,6-biphosphatase 2…: “Crystal structure of human liver 6-phosphofructo-2-KINASE/FRUCTOSE-2, 6-bisphosphatase”. X-ray diffraction, 2 ligands (AGS, PO4), 7 pockets (best druggability 0.83). MolNFT v1…

PDB
1K6M
Type
protein
Length
864 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
6-phosphofructo-2-KINASE/FRUCTOSE-2,6-biphosphatase 2- phosphatase
EC
2.7.1.105, 3.1.3.46
UniProt
P16118
Ligands
AGS, PO4
Pockets
7 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B6-phosphofructo-2-KINASE/FRUCTOSE-2,6-biphosphatase 2- phosphatase (EC 2.7.1.105, 3.1.3.46)protein43243% helix, 16% strandP16118

Ligands and binding sites

  • AGS · Phosphothiophosphoric acid-adenylate ester · ligand · 2 copies · chains A, B
  • PO4 · Phosphate ion · ion · 4 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17850.830.8690AGS
27600.830.8685AGS
31910.790.9440PO4
41820.790.9442PO4
55090.670.7850empty

Interfaces

1 interface between chains.

  • A–B · 372 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 1K6M · Crystal Structure of Human Liver 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase · the same entry in another collection · chain A against A, TM-score 1.00
  • P16118 · AlphaFold monomer V2.0 prediction for 6-phosphofructo-2-KINASE/FRUCTOSE-2,6-bisphosphatase… · a predicted model of the same protein · chain B against A, TM-score 0.99

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